1bbs: Difference between revisions
New page: left|200px<br /> <applet load="1bbs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bbs, resolution 2.8Å" /> '''X-RAY ANALYSES OF PE... |
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[[Image:1bbs.gif|left|200px]]<br /> | [[Image:1bbs.gif|left|200px]]<br /><applet load="1bbs" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1bbs, resolution 2.8Å" /> | caption="1bbs, resolution 2.8Å" /> | ||
'''X-RAY ANALYSES OF PEPTIDE INHIBITOR COMPLEXES DEFINE THE STRUCTURAL BASIS OF SPECIFICITY FOR HUMAN AND MOUSE RENINS'''<br /> | '''X-RAY ANALYSES OF PEPTIDE INHIBITOR COMPLEXES DEFINE THE STRUCTURAL BASIS OF SPECIFICITY FOR HUMAN AND MOUSE RENINS'''<br /> | ||
==Overview== | ==Overview== | ||
X-ray analyses have defined the three-dimensional structures of crystals | X-ray analyses have defined the three-dimensional structures of crystals of mouse and human renins complexed with peptide inhibitors at resolutions of 1.9 and 2.8 A, respectively. The exquisite specificity of renin arises partly from ordered loop regions at the periphery of the binding cleft. Although the pattern of main-chain hydrogen bonding in other aspartic proteinase inhibitor complexes is conserved in renins, differences in the positions of secondary structure elements (particularly helices) also lead to improved specificity in renins for angiotensinogen substrates. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1BBS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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:// | 1BBS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=1BBS OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Renin]] | [[Category: Renin]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Blundell, T | [[Category: Blundell, T L.]] | ||
[[Category: Dhanaraj, V.]] | [[Category: Dhanaraj, V.]] | ||
[[Category: aspartic proteinase]] | [[Category: aspartic proteinase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:35 2008'' | ||
Revision as of 12:53, 21 February 2008
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X-RAY ANALYSES OF PEPTIDE INHIBITOR COMPLEXES DEFINE THE STRUCTURAL BASIS OF SPECIFICITY FOR HUMAN AND MOUSE RENINS
OverviewOverview
X-ray analyses have defined the three-dimensional structures of crystals of mouse and human renins complexed with peptide inhibitors at resolutions of 1.9 and 2.8 A, respectively. The exquisite specificity of renin arises partly from ordered loop regions at the periphery of the binding cleft. Although the pattern of main-chain hydrogen bonding in other aspartic proteinase inhibitor complexes is conserved in renins, differences in the positions of secondary structure elements (particularly helices) also lead to improved specificity in renins for angiotensinogen substrates.
DiseaseDisease
Known diseases associated with this structure: Hyperproreninemia OMIM:[179820], Renal tubular dysgenesis OMIM:[179820]
About this StructureAbout this Structure
1BBS is a Single protein structure of sequence from Homo sapiens. Active as Renin, with EC number 3.4.23.15 Full crystallographic information is available from OCA.
ReferenceReference
X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins., Dhanaraj V, Dealwis CG, Frazao C, Badasso M, Sibanda BL, Tickle IJ, Cooper JB, Driessen HP, Newman M, Aguilar C, et al., Nature. 1992 Jun 11;357(6378):466-72. PMID:1608447
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