Abstract:
:Factor V(a) (FV(a)) is a cofactor for the serine protease factor X(a) that activates prothrombin to thrombin in the presence of Ca(2+) and a membrane surface. FV(a) is a heterodimer composed of one heavy chain (A1 and A2 domains) and one light chain (A3, C1, and C2 domains). We use fluorescence, circular dichroism, and equilibrium dialysis to demonstrate that (1) the FV C2 domain expressed in Sf9 cells binds one molecule of C6PS with a k(d) of approximately 2 microM, (2) stabilizing changes occur in the FV C2 domain upon C6PS binding, (3) the C6PS binding site in the FV C2 domain is located near residue Cys(2113), which reacts with DTNB, and (4) binding to a PS-containing membrane is an order of magnitude tighter than that to soluble C6PS. Coupled with a recently published crystal structure of the C2 domain, these results support a model for the mechanism of C2-membrane interaction.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Srivastava A,Quinn-Allen MA,Kim SW,Kane WH,Lentz BRdoi
10.1021/bi010449ksubject
Has Abstractpub_date
2001-07-27 00:00:00pages
8246-55issue
28eissn
0006-2960issn
1520-4995pii
bi010449kjournal_volume
40pub_type
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