1pmc
From Proteopedia
(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...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1pmc.gif|left|200px]]<br /><applet load="1pmc" size=" | + | [[Image:1pmc.gif|left|200px]]<br /><applet load="1pmc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pmc" /> | caption="1pmc" /> | ||
'''PROTEINASE INHIBITOR PMP-C (NMR, 36 STRUCTURES)'''<br /> | '''PROTEINASE INHIBITOR PMP-C (NMR, 36 STRUCTURES)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution structure and the disulfide pairings of a 36-residue | + | 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== | ==About this Structure== | ||
| - | 1PMC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Locusta_migratoria Locusta migratoria]. Full crystallographic information is available from [http:// | + | 1PMC is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hietter, H.]] | [[Category: Hietter, H.]] | ||
| - | [[Category: Lefevre, J | + | [[Category: Lefevre, J F.]] |
[[Category: Mer, G.]] | [[Category: Mer, G.]] | ||
[[Category: calcium channel blocker]] | [[Category: calcium channel blocker]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:20 2008'' |
Revision as of 12:30, 21 February 2008
|
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 Thu Feb 21 14:30:20 2008
