2ren: Difference between revisions

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[[Image:2ren.~~jpg~~|left|200px]]

[[Image:2ren.png|left|200px]]

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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==~~

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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

(as it appears on PubMed at http://www.pubmed.gov), where 2493678 is the PubMed ID number.

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==About this Structure==

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[[Category: James, M N.G.]]

[[Category: Sielecki, A R.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 16~~:45:11 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:25:57 2008''

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-[[Image:2ren.jpg|left|200px]]
+{{Seed}}
+[[Image:2ren.png|left|200px]]
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 {{STRUCTURE_2ren|  PDB=2ren  |  SCENE=  }}
-'''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
+(as it appears on PubMed at http://www.pubmed.gov), where 2493678 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_2493678}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: James, M N.G.]]
 [[Category: Sielecki, A R.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 16:45:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:25:57 2008''