1CFA

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

1CFA の概要

• エントリーDOI: 10.2210/pdb1cfa/pdb
• 分子名称: COMPLEMENT 5A SEMI-SYNTHETIC ANTAGONIST, SYNTHETIC N-TERMINAL TAIL (2 entities in total)
• 機能のキーワード: complement factor, complement alternate pathway, glycoprotein, aggregation inhibitor, gp antagonist, complement factor-peptide complex, immune system-inhibitor complex, immune system/inhibitor
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8398.88

構造登録者

Zhang, X.,Boyar, W.,Galakatos, N.,Gonnella, N.C. (登録日: 1996-09-21, 公開日: 1997-09-17, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

SOLUTION NMR