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PKD Domain
PKD (Polycystic Kidney Disease) domain was first identified in the polycystic kidney disease protein, polycystin-1 (PKD1 gene), and contains an Ig-like fold consisting of a beta-sandwich of seven strands in two sheets with a Greek key topology, although some members have additional strands. Polycystin-1 is a large cell-surface glycoprotein involved in adhesive protein–protein and protein–carbohydrate interactions; however it is not clear if the PKD domain mediates any of these interactions. PKD domains are also found in other proteins, usually in the extracellular parts of proteins involved in interactions with other proteins. For example, domains with a PKD-type fold are found in archaeal S-layer proteins that protect the cell from extreme environments, and in the human receptor SorCS2. Human proteins containing this domain GPNMB; PKD1 Polycystin 1 (often abbreviated to PC1) is a protein that in humans is encoded by the ''PKD1'' gene. Mutations of ''PKD1'' are associa ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Polycystic Kidney Disease
Polycystic kidney disease (PKD or PCKD, also known as polycystic kidney syndrome) is a genetic disorder in which the renal tubules become structurally abnormal, resulting in the development and growth of multiple cysts within the kidney. These cysts may begin to develop in utero, in infancy, in childhood, or in adulthood. Cysts are non-functioning tubules filled with fluid pumped into them, which range in size from microscopic to enormous, crushing adjacent normal tubules and eventually rendering them non-functional as well. PKD is caused by abnormal genes that produce a specific abnormal protein; this protein has an adverse effect on tubule development. PKD is a general term for two types, each having their own pathology and genetic cause: autosomal dominant polycystic kidney disease (ADPKD) and autosomal recessive polycystic kidney disease (ARPKD). The abnormal gene exists in all cells in the body; as a result, cysts may occur in the liver, seminal vesicles, and pancreas. This ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Polycystin 1
Polycystin 1 (often abbreviated to PC1) is a protein that in humans is encoded by the ''PKD1'' gene. Mutations of ''PKD1'' are associated with most cases of autosomal dominant polycystic kidney disease, a severe hereditary disorder of the kidneys characterised by the development of renal cysts and severe kidney dysfunction. Protein structure and function PC1 is a membrane-bound protein 4303 amino acids in length expressed largely upon the primary cilium, as well as apical membranes, adherens junctions, and desmosomes. It has 11 transmembrane domains, a large extracellular N-terminal domain, and a short (about 200 amino acid) cytoplasmic C-terminal domain. This intracellular domain contains a coiled-coil domain through which PC1 interacts with polycystin 2 (PC2), a membrane-bound Ca2+-permeable ion channel. PC1 has been proposed to act as a G protein–coupled receptor. The C-terminal domain may be cleaved in a number of different ways. In one instance, a ~35 kDa portion of t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ig-like Fold
The immunoglobulin superfamily (IgSF) is a large protein superfamily of cell surface and soluble proteins that are involved in the recognition, binding, or adhesion processes of cells. Molecules are categorized as members of this superfamily based on shared structural features with immunoglobulins (also known as antibodies); they all possess a domain known as an immunoglobulin domain or fold. Members of the IgSF include cell surface antigen receptors, co-receptors and co-stimulatory molecules of the immune system, molecules involved in antigen presentation to lymphocytes, cell adhesion molecules, certain cytokine receptors and intracellular muscle proteins. They are commonly associated with roles in the immune system. Otherwise, the sperm-specific protein IZUMO1, a member of the immunoglobulin superfamily, has also been identified as the only sperm membrane protein essential for sperm-egg fusion. Immunoglobulin domains Proteins of the IgSF possess a structural domain known as a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Beta-sandwich
Beta-sandwich, β-sandwich domains consisting of 80 to 350 amino acids occur commonly in proteins. They are characterized by two opposing antiparallel beta sheets (β-sheets). The number of strands found in such domains may differ from one protein to another. β-sandwich domains are subdivided in a variety of different folds. The immunoglobulin-type fold found in antibodies (Ig-fold) consists of a sandwich arrangement of 7 and 9 antiparallel β-strands arranged in two β-sheets with a Greek-key topology. The Greek-key topology is also found in Human Transthyretin. The jelly-roll topology is found in carbohydrate binding proteins such as concanavalin A and various lectins, in the collagen binding domain of ''Staphylococcus aureus'' Adhesin and in modules that bind fibronectin as found in Tenascin (Third Fibronectin Type III Repeat). The L-type lectin domain is a variation of the jelly roll fold. The C2 domain A C2 domain is a protein structural domain involved in targeting pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Greek Key (protein Structure)
The beta sheet, (β-sheet) (also β-pleated sheet) is a common motif of the regular protein secondary structure. Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation. The supramolecular association of β-sheets has been implicated in the formation of the fibrils and protein aggregates observed in amyloidosis, notably Alzheimer's disease. History The first β-sheet structure was proposed by William Astbury in the 1930s. He proposed the idea of hydrogen bonding between the peptide bonds of parallel or antiparallel extended β-strands. However, Astbury did not have the necessary data on the bond geometry of the amino acids in order to build accurate models, especially since he did not then know that the peptide bond was planar. A refined version was p ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
S-layer
An S-layer (surface layer) is a part of the cell envelope found in almost all archaea, as well as in many types of bacteria. The S-layers of both archaea and bacteria consists of a monomolecular layer composed of only one (or, in a few cases, two) identical proteins or glycoproteins. This structure is built via self-assembly and encloses the whole cell surface. Thus, the S-layer protein can represent up to 15% of the whole protein content of a cell. S-layer proteins are poorly conserved or not conserved at all, and can differ markedly even between related species. Depending on species, the S-layers have a thickness between 5 and 25 nm and possess identical pores with 2–8 nm in diameter. The terminology “S-layer” was used the first time in 1976. The general use was accepted at the "First International Workshop on Crystalline Bacterial Cell Surface Layers, Vienna (Austria)" in 1984, and in the year 1987 S-layers were defined at the European Molecular Biology Organizati ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SorCS2
The SorCS2 ( sortilin-related Vps10p domain containing receptor 2) gene is found on chromosome 4 (4p16.1), and is composed of 28 exons. The N-terminal exons which encode the Vps10p domain are spaced by large introns. The functional receptor protein is largely present in the brain. It is 1109 amino acids long, largely neutral, and has a single transmembrane pass.... SorCS2 is a member of the mammalian Vps10p (vacuolar protein sorting 10 protein) domain family consisting of five transmembrane proteins with structural similarities: SorCS1, SorCS2, SorCS3, SorLA (sorting protein-related receptor with A-type repeats), and sortilin. SorCS2 specifically has critical roles in neuronal viability and function. Single nucleotide polymorphisms (SNPs) in the protein has been associated with a range of diseases including attention-deficit hyperactivity disorder (ADHD), bipolar disorders, and schizophrenia, and the receptor family has also been associated with Alzheimer's disease an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
GPNMB
Transmembrane glycoprotein NMB is a protein that in humans is encoded by the ''GPNMB'' gene. Two transcript variants encoding 560 and 572 amino acid isoforms have been characterized for this gene in humans. The mouse and rat orthologues of GPNMB are known as DC-HIL and Osteoactivin (OA), respectively. GPNMB is a type I transmembrane glycoprotein which shows homology to the pmel17 precursor, a melanocyte-specific protein. GPNMB has been reported to be expressed in various cell types, including: melanocytes, osteoclasts, osteoblasts, dendritic cells, and it is overexpressed in various cancer types. In melanocytic cells and osteoclasts the GPNMB gene is transcriptionally regulated by Microphthalmia-associated transcription factor. Function In osteoblast progenitor cells, Osteoactivin works as a positive regulator of osteoblast differentiation during later stages of matrix maturation and mineralization that is mediated at least in part by Bone_morphogenetic_protein_2 in a SMAD1 dep ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PKD1
Polycystin 1 (often abbreviated to PC1) is a protein that in humans is encoded by the ''PKD1'' gene. Mutations of ''PKD1'' are associated with most cases of autosomal dominant polycystic kidney disease, a severe hereditary disorder of the kidneys characterised by the development of renal cysts and severe kidney dysfunction. Protein structure and function PC1 is a membrane-bound protein 4303 amino acids in length expressed largely upon the primary cilium, as well as apical membranes, adherens junctions, and desmosomes. It has 11 transmembrane domains, a large extracellular N-terminal domain, and a short (about 200 amino acid) cytoplasmic C-terminal domain. This intracellular domain contains a coiled-coil domain through which PC1 interacts with polycystin 2 (PC2), a membrane-bound Ca2+-permeable ion channel. PC1 has been proposed to act as a G protein–coupled receptor. The C-terminal domain may be cleaved in a number of different ways. In one instance, a ~35 kDa portion of t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PKD1L1
Polycystin 1 like 1, transient receptor potential channel interacting is a protein that in humans is encoded by the PKD1L1 gene. Function This gene encodes a member of the polycystin protein family containing 11 transmembrane domains, a receptor for egg jelly (REJ) domain, and a polycystin-1, lipoxygenase, alpha-toxin (PLAT) domain. The encoded protein may play a role in the male reproductive system The male reproductive system consists of a number of sex organs that play a role in the process of human reproduction. These organs are located on the outside of the body and within the pelvis. The main male sex organs are the penis and the tes .... Alternative splice variants have been described but their biological nature has not been determined. rovided by RefSeq, Jul 2008 References Further reading * {{gene-7-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PMEL (gene)
Melanocyte protein PMEL also known as premelanosome protein (PMEL) or silver locus protein homolog (SILV) is a protein that in humans is encoded by the ''PMEL'' gene. Its gene product may be referred to as PMEL, silver, ME20, gp100 or Pmel17. Structure and function PMEL is a 100 kDa type I transmembrane glycoprotein that is expressed primarily in pigment cells of the skin and eye. The transmembrane form of PMEL is modified in the secretory pathway by elaboration of N-linked oligosaccharides and addition and modification of O-linked oligosaccharides. It is then targeted to precursors of the pigment organelle, the melanosome, where it is proteolytically processed to several small fragments. Some of these fragments form non-pathological amyloid that assemble into sheets and form the striated pattern that underlies melanosomal ultrastructure. PMEL cleavage is mediated by several proteases including a proprotein convertase of the furin family, a "sheddase" that might include member ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
