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WH1 Domain
WH1 domain is an evolutionary conserved protein domain. Therefore, it has an important function. Function WH1 domains are found on WASP proteins, which are often involved in actin polymerization. Hence, WH1 is important for all cellular processes involving actin, this includes cell motility, cell trafficking, cell division and cytokinesis, cell signalling, and the establishment and maintenance of cell junctions and cell shape. Structure Tertiary structure of the WH1 domain of the Mena protein revealed structure similarities with the pleckstrin (PH) domain. The overall fold consists of a compact parallel beta-sandwich, closed along one edge by a long alpha helix. A highly conserved cluster of three surface-exposed aromatic side-chains forms the recognition site for the molecule's target ligands. Interactions The WASP protein family control actin polymerization by activating the Arp2/3 complex. WASP is defective in Wiskott–Ald ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Domain
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer aft ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Saccharomyces Cerevisiae
''Saccharomyces cerevisiae'' () (brewer's yeast or baker's yeast) is a species of yeast (single-celled fungus microorganisms). The species has been instrumental in winemaking, baking, and brewing since ancient times. It is believed to have been originally isolated from the skin of grapes. It is one of the most intensively studied eukaryotic model organisms in molecular biology, molecular and cell biology, much like ''Escherichia coli'' as the model bacteria, bacterium. It is the microorganism behind the most common type of fermentation (biochemistry), fermentation. ''S. cerevisiae'' cells are round to ovoid, 5–10 micrometre, μm in diameter. It reproduces by budding. Many proteins important in human biology were first discovered by studying their Homology (biology), homologs in yeast; these proteins include cell cycle proteins, signaling proteins, and protein-processing enzymes. ''S. cerevisiae'' is currently the only yeast cell known to have Berkeley body, Berkeley bo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Wiskott–Aldrich Syndrome Protein
The Wiskott–Aldrich Syndrome protein (WASp) is a 502-amino acid protein expressed in cells of the hematopoietic system that in humans is encoded by the ''WAS'' gene. In the inactive state, WASp exists in an autoinhibited conformation with sequences near its C-terminus binding to a region near its N-terminus. Its activation is dependent upon CDC42 and PIP2 acting to disrupt this interaction, causing the WASp protein to 'open'. This exposes a domain near the WASp C-terminus that binds to and activates the Arp2/3 complex. Activated Arp2/3 nucleates new F-actin. WASp is the founding member of a gene family which also includes the broadly expressed N-WASP (neuronal Wiskott–Aldrich Syndrome protein), SCAR/ WAVE1, WASH, WHAMM, and JMY. WAML (WASP and MIM like), WAWH (WASP without WH1 domain), and WHIMP (WAVE Homology in Membrane Protrusions) have more recently been discovered. Structure and function The Wiskott–Aldrich syndrome (WAS) family of proteins share similar dom ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Vasodilator-stimulated Phosphoprotein
Vasodilator-stimulated phosphoprotein is a protein that in humans is encoded by the ''VASP'' gene. Function Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an N-terminal EVH1 domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions cell membranes. In the mid-region of the protein, family members have a proline-rich region that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG. Interactions Vasodilator-stimulated phosphoprotein has been shown to interact with Zyxin, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SPRED3
Sprouty-related, EVH1 domain-containing protein 3 also known as Spread-3 is a protein that in humans is encoded by the ''SPRED3'' gene. Spread-3 is a member of the Sprouty (see SPRY1/SPRED) family of proteins that regulate growth factor A growth factor is a naturally occurring substance capable of stimulating cell proliferation, wound healing, and occasionally cellular differentiation. Usually it is a secreted protein or a steroid hormone. Growth factors are important for regu ...-induced activation of the MAP kinase cascade. References Further reading * * * * EVH1 domain SPR domain {{gene-19-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SPRED2
Sprouty-related, EVH1 domain-containing protein 2 is a protein that in humans is encoded by the ''SPRED2'' gene. Function SPRED2 is a member of the Sprouty (see SPRY1)/SPRED family of proteins that regulate growth factor-induced activation of the MAP kinase cascade (see MAPK1 Mitogen-activated protein kinase 1, (MAPK 1), also known as ERK2, is an enzyme that in humans is encoded by the ''MAPK1'' gene. Function The protein encoded by this gene is a member of the MAP kinase family. MAP kinases, also known as extracel ...). References Further reading * * * * * * * * * * * * * * * External links GeneReviews/NIH/NCBI/UW entry on Legius syndrome SPRED1 Sprouty-related, EVH1 domain-containing protein 1 SPR domain EVH1 domain Human proteins {{gene-2-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SPRED1
Sprouty-related, EVH1 domain-containing protein 1 (Spread-1) is a protein that in humans is encoded by the ''SPRED1'' gene located on chromosome 15q13.2 and has seven coding exons. Function SPRED-1 is a member of the Sprouty family of proteins and is phosphorylated by tyrosine kinase in response to several growth factors. The encoded protein can act as a homodimer or as a heterodimer with SPRED2 to regulate activation of the MAP kinase cascade. Clinical associations Defects in this gene are a cause of neurofibromatosis type 1-like syndrome (NFLS). Mutations in this gene are associated with * Legius syndrome. * * Childhood leukemia Mutations The following mutations have been observed: * An exon 3 c.46C>T mutation leading to p.Arg16Stop. This mutation may result in a truncated nonfunctional protein. Blast cells analysis displayed the same abnormality as germline mutation with one mutated allele (no somatic SPRED1 single-point mutation or loss of heterozygosity was found). ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
HOMER3
Homer protein homolog 3 is a protein that in humans is encoded by the ''HOMER3'' gene. Function This gene encodes a member of the homer family of dendritic proteins. Members of this family regulate group 1 metabotrophic glutamate receptor function. The encoded protein may be involved in cell growth. Interactions HOMER3 has been shown to interact with TRPC1 Transient receptor potential canonical 1 (TRPC1) is a protein that in humans is encoded by the ''TRPC1'' gene. Function TRPC1 is an ion channel located on the plasma membrane of numerous human and animal cell types. It is a nonspecific cation ... and RYR1. See also * HOMER1 * HOMER2 References Further reading * * * * * * * EVH1 domain {{gene-19-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
HOMER2
Homer protein homolog 2 is a protein that in humans is encoded by the ''HOMER2'' gene. This gene encodes a member of the homer family of dendritic proteins. Members of this family regulate group 1 metabotrophic glutamate receptor function. The encoded protein may be involved in cell growth. Four transcript variants encoding distinct isoforms have been identified for this gene. Interactions HOMER2 has been shown to interact with RYR1. See also * HOMER1 Homer protein homolog 1 or Homer1 is a neuronal protein that in humans is encoded by the ''HOMER1'' gene. Other names are Vesl and PSD-Zip45. Structure Homer1 protein has an N-terminal EVH1 domain, involved in protein interaction, and a C-te ... * HOMER3 References Further reading * * * * * * * * * * {{gene-15-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
HOMER1
Homer protein homolog 1 or Homer1 is a neuronal protein that in humans is encoded by the ''HOMER1'' gene. Other names are Vesl and PSD-Zip45. Structure Homer1 protein has an N-terminal EVH1 domain, involved in protein interaction, and a C-terminal coiled-coil domain involved in self association. It consists of two major splice variants, short-form (Homer1a) and long-form (Homer1b and c). Homer1a has only EVH1 domain and is monomeric while Homer1b and 1c have both EVH1 and coiled-coil domains and are tetrameric. The coiled-coil can be further separated into N-terminal half and C-terminal half. The N-terminal half of the coiled-coil domain is predicted to be a parallel dimer while the C-terminus half is a hybrid of dimeric and anti-parallel tetrameric coiled-coil. As a whole, long Homer is predicted to have a dumbbell-like structure where two pairs of EVH1 domains are located on two sides of long (~50 nm) coiled-coil domain. Mammals have HOMER2, Homer2 and HOMER3, Home ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enah/Vasp-like
Ena/VASP-like protein is a member of the Ena/VASP family of proteins that in humans is encoded by the ''EVL'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a ba .... References Further reading * * * * * * * * * * * * * * * * * * {{gene-14-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Motif
In a chain-like biological molecule, such as a protein or nucleic acid, a structural motif is a common three-dimensional structure that appears in a variety of different, evolutionarily unrelated molecules. A structural motif does not have to be associated with a sequence motif; it can be represented by different and completely unrelated sequences in different proteins or RNA. In nucleic acids Depending upon the sequence and other conditions, nucleic acids can form a variety of structural motifs which is thought to have biological significance. ;Stem-loop: Stem-loop intramolecular base pairing is a pattern that can occur in single-stranded DNA or, more commonly, in RNA. The structure is also known as a hairpin or hairpin loop. It occurs when two regions of the same strand, usually complementary in nucleotide sequence when read in opposite directions, base-pair to form a double helix that ends in an unpaired loop. The resulting structure is a key building block of many ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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