1pmc
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(New page: 200px<br /><applet load="1pmc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pmc" /> '''PROTEINASE INHIBITOR PMP-C (NMR, 36 STRUCTUR...)
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Revision as of 21:48, 20 November 2007
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PROTEINASE INHIBITOR PMP-C (NMR, 36 STRUCTURES)
Overview
The solution structure and the disulfide pairings of a 36-residue, proteinase inhibitor isolated from the insect Locusta migratoria have been, determined using NMR spectroscopy and simulated annealing calculations., The peptide, termed PMP-C, was previously shown to inhibit bovine, alpha-chymotrypsin as well as human leukocyte elastase, and was also found, to block high-voltage-activated Ca2+ currents in rat sensory neurones., PMP-C has a prolate ellipsoid shape and adopts a tertiary fold hitherto, unobserved in the large group of small "canonical" proteinase inhibitors., The over-all fold consists mainly of three strands arranged in a, right-handed twisted, antiparallel, beta-sheet that demarcates a cavity, together with a linear amino-terminal segment oriented almost, perpendicular to the three strands of the beta-sheet. Inside the cavity a, phenyl ring constitutes the centre of a hydrophobic core. The proteinase, binding loop is located in the carboxy-terminal part of the molecule, between two cysteine residues involved in disulfide bridges. Its, conformation resembles that found in other small canonical proteinase, inhibitors. A comparison of PMP-C structure with the recently published, solution structure of the related peptide PMP-D2 shows that the most, significant differences are complementary changes involved in the, stabilization of similar folds. This comparison led us to review the, structure of PMP-D2 and to identify two salt bridges in PMP-D2.
About this Structure
1PMC is a Single protein structure of sequence from Locusta migratoria. Full crystallographic information is available from OCA.
Reference
Solution structure of PMP-C: a new fold in the group of small serine proteinase inhibitors., Mer G, Hietter H, Kellenberger C, Renatus M, Luu B, Lefevre JF, J Mol Biol. 1996 Apr 26;258(1):158-71. PMID:8613985
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