| 词条 | WH2 motif |
| 释义 |
| Symbol = WH2 | Name = WH2 motif | image = PDB 2d1k EBI.jpg | width = | caption = Ternary complex of the WH2 domain of mim with actin-dnase I[1] | Pfam= PF02205 | InterPro= IPR003124 | SMART= WH2 | Prosite = | SCOP = 1ej5 | TCDB = | OPM family= | OPM protein= }} FunctionThe WH2 motif or WH2 domain is an evolutionarily conserved sequence motif contained in proteins.[2] It is found in WASP proteins which control actin polymerisation, therefore, WH2 is important in cellular processes such as cell contractility, cell motility, cell trafficking and cell signalling.[3] MotifThe WH2 motif (for Wiskott-Aldrich syndrome homology region 2) has been shown in WAS and Scar1/WASF1 (mammalian homologue) to interact via their WH2 motifs with actin. The WH2 (WASP-Homology 2, or Wiskott-Aldrich homology 2) domain is an ~18 amino acids actin-binding motif. This domain was first recognized as an essential element for the regulation of the cytoskeleton by the mammalian Wiskott-Aldrich syndrome protein (WASP) family. WH2 proteins occur in eukaryotes from yeast to mammals, in insect viruses, and in some bacteria. The WH2 domain is found as a modular part of larger proteins; it can be associated with the WH1 or EVH1 domain and with the CRIB domain, and the WH2 domain can occur as a tandem repeat. The WH2 domain binds to actin monomers and can facilitate the assembly of actin monomers into actin filaments.[4][5] ExamplesHuman genes encoding proteins containing the WH2 motif include:
References1. ^{{PDB|2d1k}}; {{cite journal |vauthors=Lee SH, Kerff F, Chereau D, Ferron F, Klug A, Dominguez R | title = Structural basis for the actin-binding function of missing-in-metastasis | journal = Structure | volume = 15 | issue = 2 | pages = 145–55 |date=February 2007 | pmid = 17292833 | pmc = 1853380 | doi = 10.1016/j.str.2006.12.005 | url = | issn = }} {{InterPro content|IPR003124}}{{membrane-protein-stub}}2. ^{{cite journal |vauthors=Machesky LM, Insall RH | title = Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex | journal = Curr. Biol. | volume = 8 | issue = 25 | pages = 1347–56 | year = 1998 | pmid = 9889097 | doi = 10.1016/S0960-9822(98)00015-3}} 3. ^{{cite journal|vauthors=Veltman DM, Insall RH | title=WASP family proteins: their evolution and its physiological implications. | journal=Mol Biol Cell | year= 2010 | volume= 21 | issue= 16 | pages= 2880–93 | pmid=20573979 | doi=10.1091/mbc.E10-04-0372 | pmc=2921111 }} 4. ^{{cite journal |vauthors=Machesky LM, Insall RH, Volkman LE |title=WASP homology sequences in baculoviruses |journal=Trends Cell Biol. |volume=11 |issue=7 |pages=286–287 |year=2001 |pmid=11434350 |doi=10.1016/S0962-8924(01)02009-8}} 5. ^{{cite journal |vauthors=Lappalainen P, Paunola E, Mattila PK |title=WH2 domain: a small, versatile adapter for actin monomers |journal=FEBS Lett. |volume=513 |issue=1 |pages=92–97 |year=2002 |pmid=11911886 |doi=10.1016/S0014-5793(01)03242-2}} 3 : Protein domains|Protein families|Membrane proteins |
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