1cfa | pdb_00001cfa
SOLUTION STRUCTURE OF A SEMI-SYNTHETIC C5A RECEPTOR ANTAGONIST AT PH 5.2, 303K, NMR, 20 STRUCTURES
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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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