1cfa: Difference between revisions
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[[Image:1cfa.gif|left|200px]] | [[Image:1cfa.gif|left|200px]] | ||
'''SOLUTION STRUCTURE OF A SEMI-SYNTHETIC C5A RECEPTOR ANTAGONIST AT PH 5.2, 303K, NMR, 20 STRUCTURES''' | {{Structure | ||
|PDB= 1cfa |SIZE=350|CAPTION= <scene name='initialview01'>1cfa</scene> | |||
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'''SOLUTION STRUCTURE OF A SEMI-SYNTHETIC C5A RECEPTOR ANTAGONIST AT PH 5.2, 303K, NMR, 20 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CFA is a [ | 1CFA is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9007977 9007977] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: gp antagonist]] | [[Category: gp antagonist]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:23:40 2008'' | ||
Revision as of 08:23, 20 March 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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