1cfa: Difference between revisions
New page: left|200px<br /> <applet load="1cfa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cfa" /> '''SOLUTION STRUCTURE OF A SEMI-SYNTHETIC C5A ... |
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[[Image:1cfa.gif|left|200px]]<br /> | [[Image:1cfa.gif|left|200px]]<br /><applet load="1cfa" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''SOLUTION STRUCTURE OF A SEMI-SYNTHETIC C5A RECEPTOR ANTAGONIST AT PH 5.2, 303K, NMR, 20 STRUCTURES'''<br /> | '''SOLUTION STRUCTURE OF A SEMI-SYNTHETIC C5A RECEPTOR ANTAGONIST AT PH 5.2, 303K, NMR, 20 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
The tertiary structure of a unique C5a receptor antagonist was determined | The tertiary structure of a unique C5a receptor antagonist was determined by two-dimensional NMR spectroscopy. The core domain of this 8-kDa antagonist exists as an antiparallel helical bundle, similar to recombinant human (rh)-C5a. However, unlike C5a, the antagonist's C terminus was found to be conformationally restricted along a groove between helices one and four in the core domain. This conformational restriction situates C-terminal D-Arg 75 in a wedge between core residues Arg 46 and His 15. Correlation of the antagonist's tertiary structure with point mutation analysis revealed the formation of a positively charged contiguous contact surface comprised of D-Arg 75, Arg 46, Lys 49, and His 15. The significance of this surface in generating antagonist properties implies a single binding site with the C5a receptor and provides a structural template for drug design. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1CFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1CFA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFA OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Boyar, W.]] | [[Category: Boyar, W.]] | ||
[[Category: Galakatos, N.]] | [[Category: Galakatos, N.]] | ||
[[Category: Gonnella, N | [[Category: Gonnella, N C.]] | ||
[[Category: Zhang, X.]] | [[Category: Zhang, X.]] | ||
[[Category: aggregation inhibitor]] | [[Category: aggregation inhibitor]] | ||
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[[Category: gp antagonist]] | [[Category: gp antagonist]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:34 2008'' | ||
Revision as of 10:05, 21 February 2008
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SOLUTION STRUCTURE OF A SEMI-SYNTHETIC C5A RECEPTOR ANTAGONIST AT PH 5.2, 303K, NMR, 20 STRUCTURES
Overview
The tertiary structure of a unique C5a receptor antagonist was determined by two-dimensional NMR spectroscopy. The core domain of this 8-kDa antagonist exists as an antiparallel helical bundle, similar to recombinant human (rh)-C5a. However, unlike C5a, the antagonist's C terminus was found to be conformationally restricted along a groove between helices one and four in the core domain. This conformational restriction situates C-terminal D-Arg 75 in a wedge between core residues Arg 46 and His 15. Correlation of the antagonist's tertiary structure with point mutation analysis revealed the formation of a positively charged contiguous contact surface comprised of D-Arg 75, Arg 46, Lys 49, and His 15. The significance of this surface in generating antagonist properties implies a single binding site with the C5a receptor and provides a structural template for drug design.
Disease
Known disease associated with this structure: C5 deficiency OMIM:[120900]
About this Structure
1CFA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of a unique C5a semi-synthetic antagonist: implications in receptor binding., Zhang X, Boyar W, Galakatos N, Gonnella NC, Protein Sci. 1997 Jan;6(1):65-72. PMID:9007977
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