This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1pmc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1pmc.gif|left|200px]]
[[Image:1pmc.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1pmc |SIZE=350|CAPTION= <scene name='initialview01'>1pmc</scene>
+
The line below this paragraph, containing "STRUCTURE_1pmc", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND=
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1pmc| PDB=1pmc | SCENE= }}
-
|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>
+
-
}}
+
'''PROTEINASE INHIBITOR PMP-C (NMR, 36 STRUCTURES)'''
'''PROTEINASE INHIBITOR PMP-C (NMR, 36 STRUCTURES)'''
Line 28: Line 25:
[[Category: Lefevre, J F.]]
[[Category: Lefevre, J F.]]
[[Category: Mer, G.]]
[[Category: Mer, G.]]
-
[[Category: calcium channel blocker]]
+
[[Category: Calcium channel blocker]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:14:55 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:01:33 2008''
+

Revision as of 02:14, 3 May 2008

Template:STRUCTURE 1pmc

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 Sat May 3 05:14:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools