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1vpi
From Proteopedia
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Revision as of 08:28, 30 October 2007
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PHOSPHOLIPASE A2 INHIBITOR FROM VIPOXIN
Overview
The high resolution crystal structure of a natural PLA2 inhibitor has been, determined by Patterson search methods. In the heterodimeric, neurotoxic, complex, vipoxin, isolated from the venom of Bulgarian viper, PLA2, inhibitor represents the non-toxic subunit. The model was refined to a, crystallographic R-factor of 15.5% for data between 6 and 1.76 A, resolution. The packing of the inhibitor in the crystal reveals close, contacts between the molecules, which are symmetry-related by the 2-fold, axes of the lattice. These pairs associate as a crystallographic dimer, stabilized by a set of interactions, including van der Waals contacts, between residues from symmetry-related pairs, denoted as the recognition, site and the recognition surface. Residues Ph3, Trp31 and Tyr119 represent, the ... [(full description)]
About this Structure
1VPI is a [Single protein] structure of sequence from [Vipera ammodytes]. Structure known Active Site: RS. Full crystallographic information is available from [OCA].
Reference
X-ray structure at 1.76 A resolution of a polypeptide phospholipase A2 inhibitor., Devedjiev Y, Popov A, Atanasov B, Bartunik HD, J Mol Biol. 1997 Feb 14;266(1):160-72. PMID:9054978
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