2ren: Difference between revisions

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


{{Structure
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|PDB= 2ren |SIZE=350|CAPTION= <scene name='initialview01'>2ren</scene>, resolution 2.5&Aring;
The line below this paragraph, containing "STRUCTURE_2ren", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[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] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
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|DOMAIN=
{{STRUCTURE_2ren| PDB=2ren  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ren FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ren OCA], [http://www.ebi.ac.uk/pdbsum/2ren PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ren RCSB]</span>
}}


'''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'''
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[[Category: James, M N.G.]]
[[Category: James, M N.G.]]
[[Category: Sielecki, A R.]]
[[Category: Sielecki, A R.]]
[[Category: hydrolase(acid proteinase)]]
''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 Mon Mar 31 04:59:50 2008''

Revision as of 16:45, 4 May 2008

File:2ren.jpg

Template:STRUCTURE 2ren

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


OverviewOverview

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.

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 Page seeded by OCA on Sun May 4 16:45:11 2008

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