1GNH

HUMAN C-REACTIVE PROTEIN

Summary for 1GNH

• Entry DOI: 10.2210/pdb1gnh/pdb
• Descriptor: C-REACTIVE PROTEIN, CALCIUM ION (2 entities in total)
• Functional Keywords: pentraxin, acute-phase reactant, acute-phase protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02741
• Total number of polymer chains: 10
• Total formula weight: 231321.64

Authors

Shrive, A.K.,Cheetham, G.M.T.,Holden, D.,Myles, D.A.,Turnell, W.G.,Volanakis, J.E.,Pepys, M.B.,Bloomer, A.C.,Greenhough, T.J. (deposition date: 1996-03-01, release date: 1997-01-27, Last modification date: 2024-11-13)

Primary citation

Shrive, A.K.,Cheetham, G.M.,Holden, D.,Myles, D.A.,Turnell, W.G.,Volanakis, J.E.,Pepys, M.B.,Bloomer, A.C.,Greenhough, T.J.
Three dimensional structure of human C-reactive protein.
Nat.Struct.Biol., 3:346-354, 1996

PubMed Abstract: 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.

PubMed: 8599761
DOI: 10.1038/nsb0496-346

Experimental method

X-RAY DIFFRACTION (3 Å)