NDLI: Solution structure of a unique C5a semi-synthetic antagonist: implications in receptor binding.

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Solution structure of a unique C5a semi-synthetic antagonist: implications in receptor binding.

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Solution structure of a unique C5a semi-synthetic antagonist: implications in receptor binding.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Galakatos, N. Gonnella, N. C. Boyar, W. Zhang, X.
Description	Country affiliation: United States Author Affiliation: Zhang X ( Ciba-Geigy Corporation, Pharmaceuticals Division, Summit, New Jersey 07901, USA.)
Abstract	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.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	1
Volume Number	6
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1997-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Antigens, Cd Physiology Complement C5a Metabolism Receptors, Complement Antagonists & Inhibitors Amino Acid Sequence Genetics Drug Design Magnetic Resonance Spectroscopy Molecular Sequence Data Mutagenesis Protein Structure, Tertiary Receptor, Anaphylatoxin C5a Recombinant Proteins Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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