2ren: Difference between revisions

Revision as of 08:26, 29 July 2008

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File:2ren.png

Template:STRUCTURE 2ren

STRUCTURE OF RECOMBINANT HUMAN RENIN, A TARGET FOR CARDIOVASCULAR-ACTIVE DRUGS, AT 2.5 ANGSTROMS RESOLUTIONSTRUCTURE OF RECOMBINANT HUMAN RENIN, A TARGET FOR CARDIOVASCULAR-ACTIVE DRUGS, AT 2.5 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 2493678

About this StructureAbout this Structure

2REN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of recombinant human renin, a target for cardiovascular-active drugs, at 2.5 A resolution., Sielecki AR, Hayakawa K, Fujinaga M, Murphy ME, Fraser M, Muir AK, Carilli CT, Lewicki JA, Baxter JD, James MN, Science. 1989 Mar 10;243(4896):1346-51. PMID:2493678

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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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-'''STRUCTURE OF RECOMBINANT HUMAN RENIN, A TARGET FOR CARDIOVASCULAR-ACTIVE DRUGS, AT 2.5 ANGSTROMS RESOLUTION'''
+===STRUCTURE OF RECOMBINANT HUMAN RENIN, A TARGET FOR CARDIOVASCULAR-ACTIVE DRUGS, AT 2.5 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-The x-ray crystal structure of recombinant human renin has been determined. Molecular dynamics techniques that included crystallographic data as a restraint were used to improve an initial model based on porcine pepsinogen. The present agreement factor for data from 8.0 to 2.5 angstroms (A) is 0.236. Some of the surface loops are poorly determined, and these disordered regions border a 30 A wide solvent channel. Comparison of renin with other aspartyl proteinases shows that, although the structural cores and active sites are highly conserved, surface residues, some of which are critical for specificity, vary greatly (up to 10A). Knowledge of the actual structure, as opposed to the use of models based on related enzymes, should facilitate the design of renin inhibitors.
+The line below this paragraph, {{ABSTRACT_PUBMED_2493678}}, adds the Publication Abstract to the page
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 [[Category: James, M N.G.]]
 [[Category: Sielecki, A R.]]
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