3PVO
Monoclinic form of Human C-Reactive Protein
Summary for 3PVO
| Entry DOI | 10.2210/pdb3pvo/pdb |
| Related | 1LJ7 3PVN |
| Descriptor | C-Reactive Protein, CALCIUM ION (3 entities in total) |
| Functional Keywords | pentraxin family, immune system |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P02741 |
| Total number of polymer chains | 20 |
| Total formula weight | 462963.90 |
| Authors | Guillon, C.,Mavoungou Bigouagou, U.,Jeannin, P.,Delneste, Y.,Gouet, P. (deposition date: 2010-12-07, release date: 2012-01-11, Last modification date: 2024-10-09) |
| Primary citation | Guillon, C.,Bigouagou, U.M.,Folio, C.,Jeannin, P.,Delneste, Y.,Gouet, P. A Staggered Decameric Assembly of Human C-Reactive Protein Stabilized by Zinc Ions Revealed by X-ray Crystallography. Protein Pept.Lett., 22:248-255, 2014 Cited by PubMed Abstract: Human C-reactive protein (CRP) is an acute phase protein, which harbours both host defence and scavenging properties. In this study, we obtained two new crystal forms of CRP, where CRP forms a symmetric, staggered dimer of pentamers. In one of these structures, obtained in the presence of HIV-1 Tat protein, this dimer of pentamers is stabilized by two zinc ions trapped within a cleft of the effector face of CRP. These two decameric interfaces involve complementary surfaces of CRP pentamers and bury a large area of ~2000 Å(2) per pentamer, suggesting a biological role of this interface. These two novel decameric interfaces and the involvement of zinc might have important consequences in the understanding of CRP biological functions. PubMed: 25552313PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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