2ren
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(New page: 200px<br /> <applet load="2ren" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ren, resolution 2.5Å" /> '''STRUCTURE OF RECOMBI...)
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Revision as of 21:30, 12 November 2007
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STRUCTURE OF RECOMBINANT HUMAN RENIN, A TARGET FOR CARDIOVASCULAR-ACTIVE DRUGS, AT 2.5 ANGSTROMS RESOLUTION
Contents |
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.
Disease
Known diseases associated with this structure: Hyperproreninemia OMIM:[179820], Renal tubular dysgenesis OMIM:[179820]
About this Structure
2REN is a Single protein structure of sequence from Homo sapiens with NAG as ligand. Active as Renin, with EC number 3.4.23.15 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 12 23:36:59 2007
