3CML
Crystal Structure of the DBL3x domain of the Plasmodium falcipurum VAR2CSA protein
Summary for 3CML
| Entry DOI | 10.2210/pdb3cml/pdb |
| Descriptor | Erythrocyte membrane protein 1 (2 entities in total) |
| Functional Keywords | dbl3x, var2csa, chondroitin-sulfate binding domain, membrane protein |
| Biological source | Plasmodium falciparum (malaria parasite) |
| Total number of polymer chains | 1 |
| Total formula weight | 41460.73 |
| Authors | Singh, K.,Gittis, A.G.,Nguyen, P.,Gowda, D.C.,Miller, L.H.,Garboczi, D.N. (deposition date: 2008-03-23, release date: 2008-09-02, Last modification date: 2024-10-30) |
| Primary citation | Singh, K.,Gittis, A.G.,Nguyen, P.,Gowda, D.C.,Miller, L.H.,Garboczi, D.N. Structure of the DBL3x domain of pregnancy-associated malaria protein VAR2CSA complexed with chondroitin sulfate A. Nat.Struct.Mol.Biol., 15:932-938, 2008 Cited by PubMed Abstract: Plasmodium falciparum-infected erythrocytes bind to chondroitin sulfate A (CSA) in the placenta via the VAR2CSA protein, a member of the P. falciparum erythrocyte membrane protein-1 family, leading to life-threatening malaria in pregnant women with severe effects on their fetuses and newborns. Here we describe the structure of the CSA binding DBL3x domain, a Duffy binding-like (DBL) domain of VAR2CSA. By forming a complex of DBL3x with CSA oligosaccharides and determining its structure, we have identified the CSA binding site to be a cluster of conserved positively charged residues on subdomain 2 and subdomain 3. Mutation or chemical modification of lysine residues at the site markedly diminished CSA binding to DBL3x. The location of the CSA binding site is an important step forward in the molecular understanding of pregnancy-associated malaria and offers a new target for vaccine development. PubMed: 19172746DOI: 10.1038/nsmb1479 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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