1gyk

From Proteopedia

Revision as of 13:18, 30 October 2007

SERUM AMYLOID P COMPONENT CO-CRYSTALLISED WITH MOBDG AT NEUTRAL PH

Overview

Two monoclinic (P2(1)) crystal forms of human serum amyloid P component, (SAP) in complex with the 4,6-pyruvate acetal of beta-D-galactose, (MObetaDG) were prepared. Structure analysis by molecular replacement and, refinement at 2.2A resolution revealed that crystal form 1 (a=95.76A, b=70.53A, c=103.41A, beta=96.80 degrees) contained a pentamer in the, asymmetric unit with a structure very similar to that of the published, search model. The mode of ligand co-ordination was also similar except, that four of the five subunits showed bound ligand with an additional, H-bond between O1 of the galactose and the side-chain of Lys79. One, sub-unit showed no bound ligand and a vacant calcium site close to a, crystal contact. The 2.6A resolution structure of crystal form 2, (a=118.60A, b=109.10A, ... [(full description)]

About this Structure

1GYK is a [Single protein] structure of sequence from [Homo sapiens] with CA and CDG as [ligands]. Structure known Active Site: CA1. Full crystallographic information is available from [OCA].

Reference

The structures of crystalline complexes of human serum amyloid P component with its carbohydrate ligand, the cyclic pyruvate acetal of galactose., Thompson D, Pepys MB, Tickle I, Wood S, J Mol Biol. 2002 Jul 26;320(5):1081-6. PMID:12126626

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