1aut
HUMAN ACTIVATED PROTEIN C
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OverviewOverview
The structure of the Gla-domainless form of the human anticoagulant enzyme, activated protein C has been solved at 2.8 A resolution. The light chain, is composed of two domains: an epidermal growth factor (EGF)-like domain, modified by a large insert containing an additional disulfide, followed by, a typical EGF-like domain. The arrangement of the long axis of these, domains describes an angle of approximately 80 degrees. Disulfide linked, to the light chain is the catalytic domain, which is generally, trypsin-like but contains a large insertion loop at the edge of the active, site, a third helical segment, a prominent cationic patch analogous to the, anion binding exosite I of thrombin and a trypsin-like Ca[II] binding, site. The arrangement of loops around the active site partially restricts, access to the cleft. The S2 and S4 subsites are much more polar than in, factor Xa and thrombin, and the S2 site is unrestricted. While quite open, and exposed, the active site contains a prominent groove, the surface of, which is very polar with evidence for binding sites on the primed side, in, addition to those typical of the trypsin class found on the non-primed, side.
DiseaseDisease
Known diseases associated with this structure: Purpura fulminans, neonatal OMIM:[176860], Thrombophilia due to protein C deficiency OMIM:[176860]
About this StructureAbout this Structure
1AUT is a Single protein structure of sequence from Homo sapiens. Active as Protein C (activated), with EC number 3.4.21.69 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
The 2.8 A crystal structure of Gla-domainless activated protein C., Mather T, Oganessyan V, Hof P, Huber R, Foundling S, Esmon C, Bode W, EMBO J. 1996 Dec 16;15(24):6822-31. PMID:9003757
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