2rel: Difference between revisions

Revision as of 15:30, 28 July 2008

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File:2rel.png

Template:STRUCTURE 2rel

SOLUTION STRUCTURE OF R-ELAFIN, A SPECIFIC INHIBITOR OF ELASTASE, NMR, 11 STRUCTURESSOLUTION STRUCTURE OF R-ELAFIN, A SPECIFIC INHIBITOR OF ELASTASE, NMR, 11 STRUCTURES

Template:ABSTRACT PUBMED 9171290

About this StructureAbout this Structure

2REL is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1rel. Full experimental information is available from OCA.

ReferenceReference

Solution structure of R-elafin, a specific inhibitor of elastase., Francart C, Dauchez M, Alix AJ, Lippens G, J Mol Biol. 1997 May 9;268(3):666-77. PMID:9171290

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2rel.gif|left|200px]]
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 {{STRUCTURE_2rel|  PDB=2rel  |  SCENE=  }}
-'''SOLUTION STRUCTURE OF R-ELAFIN, A SPECIFIC INHIBITOR OF ELASTASE, NMR, 11 STRUCTURES'''
+===SOLUTION STRUCTURE OF R-ELAFIN, A SPECIFIC INHIBITOR OF ELASTASE, NMR, 11 STRUCTURES===
-==Overview==
+<!--
-The solution structure of r-elafin, a specific elastase inhibitor, has been determined using NMR spectroscopy. Characterized by a flat core and a flexible N-terminal extremity, the three-dimensional structure is formed by a central twisted beta-hairpin accompanied by two external segments linked by the proteinase binding loop. A cluster of three disulfide bridges connects the external segments to the central beta-sheet and a single fourth disulfide bridge links the binding loop to the central beta-turn. The same spatial distribution of disulfide bridges can be observed in both domains of the secretory leukocyte protease inhibitor (SLPI), another elastase inhibitor. The structural homology between r-elafin and the C-terminal domain of SLPI confirms the former as a second member of the chelonianin family of proteinase inhibitors. Based on the homology between the two proteins and recent results obtained for elastase binding mutants of the bovine pancreatic trypsin inhibitor (BPTI), we define the segment 22 to 27 as the binding loop of elafin, with the scissile peptide bond between Ala24 and Met25. In our solution structures, this loop is extended and solvent-exposed, and exhibits a large degree of flexibility. This mobility, already observed for the binding loop in other protease inhibitors in solution, might be an important feature for the interaction with the corresponding protease.
+The line below this paragraph, {{ABSTRACT_PUBMED_9171290}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9171290 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9171290}}
 ==About this Structure==
-REL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1rel 1rel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REL OCA].
+REL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1rel 1rel]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REL OCA].
 ==Reference==
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 [[Category: R-elafin]]
 [[Category: Serine protease inhibitor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 16:45:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:30:06 2008''