1pmc: Difference between revisions
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== | ==PROTEINASE INHIBITOR PMP-C (NMR, 36 STRUCTURES)== | ||
<StructureSection load='1pmc' size='340' side='right'caption='[[1pmc]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1pmc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Locusta_migratoria Locusta migratoria]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PMC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 36 models</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pmc OCA], [https://pdbe.org/1pmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pmc RCSB], [https://www.ebi.ac.uk/pdbsum/1pmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pmc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LCM_LOCMI LCM_LOCMI] Both LCMI I and II are inhibitors of chymotrypsin and elastase (in vitro). They both inhibit the prophenol oxidase activation cascade. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | 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. | ||
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<ref>PMID:8613985</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1pmc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Locusta migratoria]] | [[Category: Locusta migratoria]] | ||
[[Category: Hietter H]] | |||
[[Category: Hietter | [[Category: Lefevre J-F]] | ||
[[Category: Lefevre | [[Category: Mer G]] | ||
[[Category: Mer | |||
Latest revision as of 10:34, 23 October 2024
PROTEINASE INHIBITOR PMP-C (NMR, 36 STRUCTURES)PROTEINASE INHIBITOR PMP-C (NMR, 36 STRUCTURES)
Structural highlights
FunctionLCM_LOCMI Both LCMI I and II are inhibitors of chymotrypsin and elastase (in vitro). They both inhibit the prophenol oxidase activation cascade. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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