3vww
Crystal structure of a0-domain of P5 from H. sapiensCrystal structure of a0-domain of P5 from H. sapiens
Template:ABSTRACT PUBMED 23949117
FunctionFunction
[PDIA6_HUMAN] May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.[1] [2]
About this StructureAbout this Structure
3vww is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Sato Y, Kojima R, Okumura M, Hagiwara M, Masui S, Maegawa K, Saiki M, Horibe T, Suzuki M, Inaba K. Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding. Sci Rep. 2013 Aug 16;3:2456. doi: 10.1038/srep02456. PMID:23949117 doi:10.1038/srep02456
- ↑ Jordan PA, Stevens JM, Hubbard GP, Barrett NE, Sage T, Authi KS, Gibbins JM. A role for the thiol isomerase protein ERP5 in platelet function. Blood. 2005 Feb 15;105(4):1500-7. Epub 2004 Oct 5. PMID:15466936 doi:10.1182/blood-2004-02-0608
- ↑ Kikuchi M, Doi E, Tsujimoto I, Horibe T, Tsujimoto Y. Functional analysis of human P5, a protein disulfide isomerase homologue. J Biochem. 2002 Sep;132(3):451-5. PMID:12204115