1C5A

THREE-DIMENSIONAL STRUCTURE OF PORCINE C5ADES*ARG FROM 1H NUCLEAR MAGNETIC RESONANCE DATA

1C5A の概要

• エントリーDOI: 10.2210/pdb1c5a/pdb
• 分子名称: COMPLEMENT C5A ANAPHYLATOXIN (1 entity in total)
• 機能のキーワード: complement factor
• 由来する生物種: Sus scrofa domestica (domestic pig)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8468.85

構造登録者

Williamson, M.P.,Madison, V.S. (登録日: 1990-06-12, 公開日: 1991-10-15, 最終更新日: 2024-10-16)

主引用文献

Williamson, M.P.,Madison, V.S.
Three-dimensional structure of porcine C5adesArg from 1H nuclear magnetic resonance data.
Biochemistry, 29:2895-2905, 1990

PubMed Abstract: Two-dimensional nuclear magnetic resonance spectra of porcine C5adesArg (73 residues) have been used to construct a list of 34 hydrogen bonds, 27 dihedral angle constraints, and 151 distance constraints, derived from nuclear Overhauser effect data. These constraints were used in restrained molecular dynamics calculations on residues 1-65 of C5a, starting from a folded structure modeled on the crystal structure of a homologous protein, C3a. Forty-one structures have been calculated, which fall into three similar families with few violations of the imposed constraints. Structures in the most populated family have a root-mean-square deviation from the average structure of 1.02 A for the C alpha atoms, with good definition of the internal residues. There is good agreement between the calculated structures and other nuclear magnetic resonance data. The structure is very similar to that recently reported for human C5a [Zuiderweg et al. (1989) Biochemistry 28, 172-185]. Some biological implications of these structures are discussed.

PubMed: 2337573
DOI: 10.1021/bi00464a002

実験手法

SOLUTION NMR