1pmc
From Proteopedia
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| - | [[Image:1pmc.gif|left|200px]] | + | [[Image:1pmc.gif|left|200px]] |
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| - | '''PROTEINASE INHIBITOR PMP-C (NMR, 36 STRUCTURES)''' | + | {{Structure |
| + | |PDB= 1pmc |SIZE=350|CAPTION= <scene name='initialview01'>1pmc</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''PROTEINASE INHIBITOR PMP-C (NMR, 36 STRUCTURES)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PMC is a [ | + | 1PMC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Locusta_migratoria Locusta migratoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PMC OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8613985 8613985] |
[[Category: Locusta migratoria]] | [[Category: Locusta migratoria]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: calcium channel blocker]] | [[Category: calcium channel blocker]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:26:10 2008'' |
Revision as of 11:26, 20 March 2008
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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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