1pmc
From Proteopedia
Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pmc OCA], [http://www.ebi.ac.uk/pdbsum/1pmc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pmc RCSB]</span> | ||
}} | }} | ||
Line 27: | Line 30: | ||
[[Category: calcium channel blocker]] | [[Category: calcium channel blocker]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:01:33 2008'' |
Revision as of 20:01, 30 March 2008
| |||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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
Page seeded by OCA on Sun Mar 30 23:01:33 2008