Three dimensional structure of human C-reactive protein

Annette K. Shrive; Graham M.T. Cheetham; David Holden; Dean A.A. Myles; William G. Turnell; John E. Volanakis; Mark B. Pepys; Anne C. Bloomer; Trevor J. Greenhough

doi:10.1038/nsb0496-346

Three dimensional structure of human C-reactive protein

Annette K. Shrive, Graham M.T. Cheetham, David Holden, Dean A.A. Myles, William G. Turnell, John E. Volanakis, Mark B. Pepys, Anne C. Bloomer, Trevor J. Greenhough

Research output: Contribution to journal › Article › peer-review

319 Scopus citations

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.

Original language	English
Pages (from-to)	346-354
Number of pages	9
Journal	Nature Structural Biology
Volume	3
Issue number	4
DOIs	https://doi.org/10.1038/nsb0496-346
State	Published - Apr 1996
Externally published	Yes

Access to Document

10.1038/nsb0496-346

Cite this

@article{d3460e8e4ea34ec8b21ca423cbd3bd5f,

title = "Three dimensional structure of human C-reactive protein",

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.",

author = "Shrive, {Annette K.} and Cheetham, {Graham M.T.} and David Holden and Myles, {Dean A.A.} and Turnell, {William G.} and Volanakis, {John E.} and Pepys, {Mark B.} and Bloomer, {Anne C.} and Greenhough, {Trevor J.}",

year = "1996",

month = apr,

doi = "10.1038/nsb0496-346",

language = "English",

volume = "3",

pages = "346--354",

journal = "Nature Structural Biology",

issn = "1072-8368",

number = "4",

}

TY - JOUR

T1 - Three dimensional structure of human C-reactive protein

AU - Shrive, Annette K.

AU - Cheetham, Graham M.T.

AU - Holden, David

AU - Myles, Dean A.A.

AU - Turnell, William G.

AU - Volanakis, John E.

AU - Pepys, Mark B.

AU - Bloomer, Anne C.

AU - Greenhough, Trevor J.

PY - 1996/4

Y1 - 1996/4

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0030007457&partnerID=8YFLogxK

U2 - 10.1038/nsb0496-346

DO - 10.1038/nsb0496-346

M3 - Article

C2 - 8599761

AN - SCOPUS:0030007457

SN - 1072-8368

VL - 3

SP - 346

EP - 354

JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 4

ER -

Three dimensional structure of human C-reactive protein

Abstract

Access to Document

Other files and links

Fingerprint

Cite this