 |
PDBsum entry 1c5a
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Complement factor
|
PDB id
|
|
|
|
1c5a
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Three-Dimensional structure of porcine c5adesarg from 1h nuclear magnetic resonance data.
|
 |
|
Authors
|
 |
M.P.Williamson,
V.S.Madison.
|
 |
|
Ref.
|
 |
Biochemistry, 1990,
29,
2895-2905.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
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.
|
 |
|
Secondary reference #1
|
 |
|
Title
|
 |
1h nuclear magnetic resonance assignments and secondary structure of porcine c5ades arg.
|
 |
|
Author
|
 |
M.P.Williamson.
|
 |
|
Ref.
|
 |
J Mol Biol, 1989,
206,
407-410.
|
 |
|
PubMed id
|
 |
|
 |
 |
|
|
 |
|
|
|
|
 |