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SRP Receptor
Signal recognition particle (SRP) receptor, also called the docking protein, is a dimer composed of 2 different subunits that are associated exclusively with the rough ER in mammalian cells. Its main function is to identify the SRP units. SRP (signal recognition particle) is a molecule that helps the ribosome-mRNA-polypeptide complexes to settle down on the membrane of the endoplasmic reticulum. The eukaryotic SRP receptor (termed SR) is a heterodimer of SR-alpha (70 kDa; SRPRA) and SR-beta (25 kDa; SRPRB), both of which contain a GTP-binding domain, while the prokaryotic SRP receptor comprises only the monomeric loosely membrane-associated SR-alpha homologue FtsY (). SRX domain SR-alpha regulates the targeting of SRP-ribosome-nascent polypeptide complexes to the translocon. SR-alpha binds to the SRP54 subunit of the SRP complex. The SR-beta subunit is a transmembrane GTPase that anchors the SR-alpha subunit (a peripheral membrane GTPase) to the ER membrane. SR-beta interac ...
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Protein Dimer
In biochemistry, a protein dimer is a macromolecular complex or protein multimer, multimer formed by two protein monomers, or single proteins, which are usually Non-covalent interaction, non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word ''dimer'' has roots meaning "two parts", ''wikt:di-#Prefix, di-'' + ''wikt:-mer#Suffix, -mer''. A protein dimer is a type of protein quaternary structure. A protein homodimer is formed by two identical proteins while a protein heterodimer is formed by two different proteins. Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains. An exception is dimers that are linked by disulfide bridges such as the homodimeric protein IKBKG, NEMO. Some proteins contain specialized domains to ensure dimerization (dimerization domains) and specificity. The G protein- ...
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Receptors
Receptor may refer to: *Sensory receptor, in physiology, any neurite structure that, on receiving environmental stimuli, produces an informative nerve impulse *Receptor (biochemistry), in biochemistry, a protein molecule that receives and responds to a neurotransmitter, or other substance **Cell surface receptor, a receptor on the outer surface of a cell membrane, that takes part in communication between the cell and the outside world **Nuclear receptor, a receptor found within cells that is responsible for sensing steroid and thyroid hormones and certain other molecules **Immune receptor, a receptor that occurs on the surface of immunocytes and binds to antigens *Receiver (radio) In radio, radio communications, a radio receiver, also known as a receiver, a wireless, or simply a radio, is an electronic device that receives radio waves and converts the information carried by them to a usable form. It is used with an ante ...
, a device for the reception of electromagnetic ...
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Arthritis Research & Therapy
''Arthritis Research & Therapy'', formerly ''Arthritis Research'', is a peer-reviewed open access medical journal covering the field of cellular and molecular mechanisms of arthritis, musculoskeletal conditions, and systemic autoimmune rheumatic diseases. It is published by BioMed Central, part of Springer Nature, and the editors-in-chief are Christopher Buckley (University of Birmingham and University of Oxford) and Harris Perlman (Northwestern University). The journal was established in 1999 as ''Arthritis Research'', obtaining its current title in. The journal's print version ceased in 2010 with volume 12, number 6, and the journal converted to an online only format. According to the ''Journal Citation Reports'', the journal has a 2017 impact factor The impact factor (IF) or journal impact factor (JIF) of an academic journal is a type of journal ranking. Journals with higher impact factor values are considered more prestigious or important within their field. The Impact F ...
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Signal Recognition Particle
The signal recognition particle (SRP) is an abundant, cytosolic, universally conserved ribonucleoprotein (protein-RNA complex) that recognizes and targets specific proteins to the endoplasmic reticulum in eukaryotes and the plasma membrane in prokaryotes. History The function of SRP was discovered by the study of processed and unprocessed secretory proteins, particularly immunoglobulin light chains; and bovine preprolactin. Newly synthesized proteins in eukaryotes carry N-terminal hydrophobic Signal peptide, signal sequences, which are bound by SRP when they emerge from the ribosome. Mechanism In eukaryotes, SRP binds to the Signal peptide, signal sequence of a newly synthesized peptide as it emerges from the ribosome. This binding leads to the slowing of protein synthesis known as "elongation arrest", a conserved function of SRP that facilitates the coupling of the protein Translation (genetics), translation and the protein translocation processes. SRP then targets this en ...
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GTPase
GTPases are a large family of hydrolase enzymes that bind to the nucleotide guanosine triphosphate (GTP) and hydrolyze it to guanosine diphosphate (GDP). The GTP binding and hydrolysis takes place in the highly conserved P-loop "G domain", a protein domain common to many GTPases. Functions GTPases function as molecular switches or timers in many fundamental cellular processes. Examples of these roles include: * Signal transduction in response to activation of cell surface receptors, including transmembrane receptors such as those mediating taste, smell and vision. * Protein biosynthesis (a.k.a. translation) at the ribosome. * Regulation of cell differentiation, proliferation, division and movement. * Translocation of proteins through membranes. * Transport of vesicles within the cell, and vesicle-mediated secretion and uptake, through GTPase control of vesicle coat assembly. GTPases are active when bound to GTP and inactive when bound to GDP. In the general ...
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Translocon
The translocon (also known as a translocator or translocation channel) is a complex of proteins associated with the translocation of polypeptides across membranes. In eukaryotes the term translocon most commonly refers to the complex that transports nascent polypeptides with a targeting signal sequence into the interior (cisternal or lumenal) space of the endoplasmic reticulum (ER) from the cytosol. This translocation process requires the protein to cross a hydrophobic lipid bilayer. The same complex is also used to integrate nascent proteins into the membrane itself (membrane proteins). In prokaryotes, a similar protein complex transports polypeptides across the (inner) plasma membrane or integrates membrane proteins. In either case, the protein complex is formed from Sec proteins (Sec: secretory), with the hetero-trimeric Sec61 being the channel. In prokaryotes, the homologous channel complex is known as SecYEG. This article focuses on the cell's native translocons, but pathogen ...
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SRPRB
Signal recognition particle receptor subunit beta is a protein that in humans is encoded by the ''SRPRB'' gene. The protein encoded by this gene has similarity to mouse protein which is a subunit of the signal recognition particle receptor (SR). This subunit is a transmembrane GTPase belonging to the GTPase superfamily. It anchors alpha subunit, a peripheral membrane GTPase, to the ER membrane. SR is required for the cotranslational targeting of both secretory and membrane proteins Membrane proteins are common proteins that are part of, or interact with, biological membranes. Membrane proteins fall into several broad categories depending on their location. Integral membrane proteins are a permanent part of a cell membrane ... to the ER membrane. References Further reading

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Endoplasmic Reticulum
The endoplasmic reticulum (ER) is a part of a transportation system of the eukaryote, eukaryotic cell, and has many other important functions such as protein folding. The word endoplasmic means "within the cytoplasm", and reticulum is Latin for "little net". It is a type of organelle made up of two subunits – rough endoplasmic reticulum (RER), and smooth endoplasmic reticulum (SER). The endoplasmic reticulum is found in most eukaryotic cells and forms an interconnected network of flattened, membrane-enclosed sacs known as cisternae (in the RER), and tubular structures in the SER. The membranes of the ER are continuous with the outer nuclear membrane. The endoplasmic reticulum is not found in red blood cells, or spermatozoa. There are two types of ER that share many of the same proteins and engage in certain common activities such as the synthesis of certain lipids and cholesterol. Different types of Cell (biology), cells contain different ratios of the two types of ER dependin ...
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Mammal
A mammal () is a vertebrate animal of the Class (biology), class Mammalia (). Mammals are characterised by the presence of milk-producing mammary glands for feeding their young, a broad neocortex region of the brain, fur or hair, and three Evolution of mammalian auditory ossicles, middle ear bones. These characteristics distinguish them from reptiles and birds, from which their ancestors Genetic divergence, diverged in the Carboniferous Period over 300 million years ago. Around 6,640 Neontology#Extant taxon, extant species of mammals have been described and divided into 27 Order (biology), orders. The study of mammals is called mammalogy. The largest orders of mammals, by number of species, are the rodents, bats, and eulipotyphlans (including hedgehogs, Mole (animal), moles and shrews). The next three are the primates (including humans, monkeys and lemurs), the Artiodactyl, even-toed ungulates (including pigs, camels, and whales), and the Carnivora (including Felidae, ...
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Biological Membrane
A biological membrane, biomembrane or cell membrane is a selectively permeable membrane that separates the interior of a cell from the external environment or creates intracellular compartments by serving as a boundary between one part of the cell and another. Biological membranes, in the form of eukaryotic cell membranes, consist of a phospholipid bilayer with embedded, integral and peripheral proteins used in communication and transportation of chemicals and ions. The bulk of lipids in a cell membrane provides a fluid matrix for proteins to rotate and laterally diffuse for physiological functioning. Proteins are adapted to high membrane fluidity environment of the lipid bilayer with the presence of an annular lipid shell, consisting of lipid molecules bound tightly to the surface of integral membrane proteins. The cell membranes are different from the isolating tissues formed by layers of cells, such as mucous membranes, basement membranes, and serous membranes. ...
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Polypeptide
Peptides are short chains of amino acids linked by peptide bonds. A polypeptide is a longer, continuous, unbranched peptide chain. Polypeptides that have a molecular mass of 10,000 Da or more are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. Peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others. Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligands such as coenzymes and cofactors, to another protein or other macromolecule such as DNA or RNA, or to complex macromolecular assemblies. Amino acids that have been incorporated into peptides are termed residues. A water molecule is released during formation of each amide bond.. All peptides except cyclic peptides have an N-terminal (amine group) and C-terminal (ca ...
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