1ccv
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(New page: 200px<br /><applet load="1ccv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ccv" /> '''NMR SOLUTION STRUCTURE OF APIS MELLIFERA CHY...)
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Revision as of 10:14, 20 November 2007
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NMR SOLUTION STRUCTURE OF APIS MELLIFERA CHYMOTRYPSIN INHIBITOR (AMCI).
Overview
The three-dimensional structure of the 56 residue polypeptide Apis, mellifera chymotrypsin/cathepsin G inhibitor 1 (AMCI-1) isolated from, honey bee hemolymph was calculated based on 730 experimental NMR, restraints. It consists of two approximately perpendicular beta-sheets, several turns, and a long exposed loop that includes the protease binding, site. The lack of extensive secondary structure features or hydrophobic, core is compensated by the presence of five disulfide bridges that, stabilize both the protein scaffold and the binding loop segment. A, detailed analysis of the protease binding loop conformation reveals that, it is similar to those found in other canonical serine protease, inhibitors. The AMCI-1 structure exhibits a common fold with a novel, family of inhibitors from the intestinal parasitic worm Ascaris suum. The, pH-induced conformational changes in the binding loop region observed in, the Ascaris inhibitor ATI are absent in AMCI-1. Similar binding site, sequences and structures strongly suggest that the lack of the, conformational change can be attributed to a Glu-->Gln substitution at the, P1' position in AMCI-1, compared to ATI. Analysis of amide proton, temperature coefficients shows very good correlation with the presence of, hydrogen bond donors in the calculated AMCI-1 structure.
About this Structure
1CCV is a Single protein structure of sequence from Apis mellifera. Full crystallographic information is available from OCA.
Reference
NMR solution structure of Apis mellifera chymotrypsin/cathepsin G inhibitor-1 (AMCI-1): structural similarity with Ascaris protease inhibitors., Cierpicki T, Bania J, Otlewski J, Protein Sci. 2000 May;9(5):976-84. PMID:10850807
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