2ren
From Proteopedia
(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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caption="2ren, resolution 2.5Å" /> | caption="2ren, resolution 2.5Å" /> | ||
'''STRUCTURE OF RECOMBINANT HUMAN RENIN, A TARGET FOR CARDIOVASCULAR-ACTIVE DRUGS, AT 2.5 ANGSTROMS RESOLUTION'''<br /> | '''STRUCTURE OF RECOMBINANT HUMAN RENIN, A TARGET FOR CARDIOVASCULAR-ACTIVE DRUGS, AT 2.5 ANGSTROMS RESOLUTION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2REN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Renin Renin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.15 3.4.23.15] Full crystallographic information is available from [http:// | + | 2REN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Renin Renin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.15 3.4.23.15] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2REN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase(acid proteinase)]] | [[Category: hydrolase(acid proteinase)]] | ||
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Revision as of 15:42, 15 February 2008
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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 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
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