2hlc: Difference between revisions

Revision as of 12:41, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2hlc.png

Template:STRUCTURE 2hlc

HL COLLAGENASE STRUCTURE AT 1.7A RESOLUTIONHL COLLAGENASE STRUCTURE AT 1.7A RESOLUTION

Template:ABSTRACT PUBMED 15299709

About this StructureAbout this Structure

2HLC is a Single protein structure of sequence from Hypoderma lineatum. Full crystallographic information is available from OCA.

ReferenceReference

1.8 A structure of Hypoderma lineatum collagenase: a member of the serine proteinase family., Broutin I, Arnoux B, Riche C, Lecroisey A, Keil B, Pascard C, Ducruix A, Acta Crystallogr D Biol Crystallogr. 1996 Mar 1;52(Pt 2):380-92. PMID:15299709

Page seeded by OCA on Sun Jul 27 12:41:16 2008

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OCA

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-[[Image:2hlc.gif|left|200px]]
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 {{STRUCTURE_2hlc|  PDB=2hlc  |  SCENE=  }}
-'''HL COLLAGENASE STRUCTURE AT 1.7A RESOLUTION'''
+===HL COLLAGENASE STRUCTURE AT 1.7A RESOLUTION===
-==Overview==
+<!--
-Collagenase from the fly larvae Hypoderma lineatum cleaves triple-helical collagen in a single region. It was crystallized at neutral pH in the absence of inhibitor and 1.8 A data were collected using synchrotron radiation and a Mark II prototype detector. The structure was solved by combining multiple isomorphous replacement methods and rotation translation function in real space. Refinement between 7 and 1.8 A using the program X-PLOR led to a final R factor of 16.9%. The overall fold is similar to that of other trypsin-like enzymes but the structure differs mainly by the presence of a beta-sheet at position 31-44. The two embedded molecules of the asymmetric unit are related by a pseudo twofold axis. The beta-sheet 31-44 of one molecule is involved in hydrogen bonds with binding-pocket residues of the other molecule. It thus completely prevents access to the active site. The specificity of this enzyme probably results from the position of Phe192 and Tyr99 at the entrance of the active site.
+The line below this paragraph, {{ABSTRACT_PUBMED_15299709}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15299709 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15299709}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Serine protease]]
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