1bea
From Proteopedia
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BIFUNCTIONAL HAGEMAN FACTOR/AMYLASE INHIBITOR FROM MAIZE
Overview
Corn Hageman factor inhibitor (CHFI) is a bifunctional 127 residue, 13.6, kDa protein isolated from corn seeds. It inhibits mammalian trypsin and, Factor XIIa (Hageman Factor) of the contact pathway of coagulation as well, as alpha-amylases from several insect species. Among the plasma, proteinases, CHFI specifically inhibits Factor XIIa without affecting the, activity of other coagulation proteinases. We have isolated CHFI from corn, and determined the crystallographic structure at 1.95 A resolution., Additionally, we have solved the structure of the recombinant protein, produced in Escherichia coli at 2.2 A resolution. The two proteins are, essentially identical. The proteinase binding loop is in the canonical, conformation for proteinase inhibitors. In an effort to understand, ... [(full description)]
About this Structure
1BEA is a [Single protein] structure of sequence from [Zea mays]. Structure known Active Site: SLE. Full crystallographic information is available from [OCA].
Reference
Structural determinants of the bifunctional corn Hageman factor inhibitor: x-ray crystal structure at 1.95 A resolution., Behnke CA, Yee VC, Trong IL, Pedersen LC, Stenkamp RE, Kim SS, Reeck GR, Teller DC, Biochemistry. 1998 Nov 3;37(44):15277-88. PMID:9799488
Page seeded by OCA on Tue Oct 30 14:54:29 2007
