1hle: Difference between revisions

Revision as of 08:21, 1 July 2008

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File:1hle.png

Template:STRUCTURE 1hle

CRYSTAL STRUCTURE OF CLEAVED EQUINE LEUCOCYTE ELASTASE INHIBITOR DETERMINED AT 1.95 ANGSTROMS RESOLUTIONCRYSTAL STRUCTURE OF CLEAVED EQUINE LEUCOCYTE ELASTASE INHIBITOR DETERMINED AT 1.95 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1518052

About this StructureAbout this Structure

1HLE is a Protein complex structure of sequences from Equus caballus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution., Baumann U, Bode W, Huber R, Travis J, Potempa J, J Mol Biol. 1992 Aug 20;226(4):1207-18. PMID:1518052

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OCA

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-'''CRYSTAL STRUCTURE OF CLEAVED EQUINE LEUCOCYTE ELASTASE INHIBITOR DETERMINED AT 1.95 ANGSTROMS RESOLUTION'''
+===CRYSTAL STRUCTURE OF CLEAVED EQUINE LEUCOCYTE ELASTASE INHIBITOR DETERMINED AT 1.95 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-The crystal structure of active-site cleaved equine leucocyte elastase inhibitor, a member of the serpin superfamily, has been solved and refined to a crystallographic R-factor of 17.6% at 1.95 A resolution. Despite being an intracellular inhibitor with rather low sequence homology of 30% to human alpha 1-antichymotrypsin and alpha 1-proteinase inhibitor, the three-dimensional structures are very similar, with deviations only at the sites of insertions and few mobile secondary structure elements. The better resolution in comparison with the structures of other cleaved serpins allows a more precise description of the so-called R-state of the serpins.
+The line below this paragraph, {{ABSTRACT_PUBMED_1518052}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_1518052}}
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