1C5A
THREE-DIMENSIONAL STRUCTURE OF PORCINE C5ADES*ARG FROM 1H NUCLEAR MAGNETIC RESONANCE DATA
Summary for 1C5A
| Entry DOI | 10.2210/pdb1c5a/pdb |
| Descriptor | COMPLEMENT C5A ANAPHYLATOXIN (1 entity in total) |
| Functional Keywords | complement factor |
| Biological source | Sus scrofa domestica (domestic pig) |
| Total number of polymer chains | 1 |
| Total formula weight | 8468.85 |
| Authors | Williamson, M.P.,Madison, V.S. (deposition date: 1990-06-12, release date: 1991-10-15, Last modification date: 2024-10-16) |
| Primary citation | Williamson, M.P.,Madison, V.S. Three-dimensional structure of porcine C5adesArg from 1H nuclear magnetic resonance data. Biochemistry, 29:2895-2905, 1990 Cited by 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: 2337573DOI: 10.1021/bi00464a002 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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