1CFA

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

Summary for 1CFA

• Entry DOI: 10.2210/pdb1cfa/pdb
• Descriptor: COMPLEMENT 5A SEMI-SYNTHETIC ANTAGONIST, SYNTHETIC N-TERMINAL TAIL (2 entities in total)
• Functional Keywords: complement factor, complement alternate pathway, glycoprotein, aggregation inhibitor, gp antagonist, complement factor-peptide complex, immune system-inhibitor complex, immune system/inhibitor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 8398.88

Authors

Zhang, X.,Boyar, W.,Galakatos, N.,Gonnella, N.C. (deposition date: 1996-09-21, release date: 1997-09-17, Last modification date: 2024-10-23)

Primary citation

Zhang, X.,Boyar, W.,Galakatos, N.,Gonnella, N.C.
Solution structure of a unique C5a semi-synthetic antagonist: implications in receptor binding.
Protein Sci., 6:65-72, 1997

PubMed 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.

PubMed: 9007977

Experimental method

SOLUTION NMR