Three dimensional structure of human C-reactive protein.
The structure of the classical acute phase reactant human C-reactive protein provides evidence that phosphocholine binding is mediated through calcium and a hydrophobic pocket centred on Phe 66. The residue Glu 81 is suitably positioned to interact with the choline group. A cleft on the pentameric face opposite to that containing the calcium site may have an important functional role. The structure provides insights into the molecular mechanisms by which this highly conserved plasma protein, for which no polymorphism or deficiency state is known, may exert its biological role.
Shrive
A K
AK
Department of Physics, Keele University, Keele, UK.
Cheetham
G M
GM
Holden
D
D
Myles
D A
DA
Turnell
W G
WG
Volanakis
J E
JE
Pepys
M B
MB
Bloomer
A C
AC
Greenhough
T J
TJ
D000595:Amino Acid Sequence; D002097:C-Reactive Protein / Q000737:chemistry* / Q000378:metabolism; D002118:Calcium / Q000378:metabolism; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010767:Phosphorylcholine / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D000683:Serum Amyloid P-Component / Q000737:chemistry
D000683:Serum Amyloid P-Component; D010767:Phosphorylcholine; D002097:C-Reactive Protein; D002118:Calcium