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Three dimensional structure of human C-reactive protein

A K Shrive1, G M Cheetham, D Holden

  • 1Department of Physics, Keele University, Keele, UK.

Nature Structural Biology
|April 1, 1996
PubMed

Insights

The structure of human C-reactive protein reveals how it binds phosphocholine via calcium and a hydrophobic pocket. This understanding offers insights into the protein's biological functions.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Immunology

Background:

  • Human C-reactive protein (CRP) is a classical acute phase reactant.
  • CRP plays a crucial role in the innate immune system.
  • The precise molecular mechanisms of CRP's biological functions are not fully understood.

Purpose of the Study:

  • To elucidate the structural basis of phosphocholine binding by human C-reactive protein.
  • To gain insights into the molecular mechanisms underlying CRP's biological role.

Main Methods:

  • X-ray crystallography was used to determine the structure of human C-reactive protein.
  • Structural analysis focused on identifying key residues and interactions involved in ligand binding.

Main Results:

  • The structure reveals that phosphocholine binding is mediated by calcium ions and a hydrophobic pocket involving Phe 66.
  • The residue Glu 81 is positioned to interact with the choline group.
  • A cleft on the pentameric face, opposite the calcium site, may have a significant functional role.

Conclusions:

  • The determined structure provides a molecular explanation for phosphocholine binding by CRP.
  • These findings offer valuable insights into the biological functions of this conserved plasma protein.

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