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PDBsum entry 1cfa
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Immune system/inhibitor
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PDB id
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1cfa
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Solution structure of a unique c5a semi-Synthetic antagonist: implications in receptor binding.
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Authors
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X.Zhang,
W.Boyar,
N.Galakatos,
N.C.Gonnella.
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Ref.
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Protein Sci, 1997,
6,
65-72.
[DOI no: ]
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PubMed id
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Abstract
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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.
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