5x6n

Structure of P. Knowlesi DBL Domain Capable of binding Human Duffy Antigen

spinqualitylabelsall models 5x6n, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5x6n is a 1 chain structure with sequence from Plakn. This structure supersedes the now removed PDB entry 2c6j. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BOG, SO4 Gene: dbp alpha (PLAKN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Molecular processes that govern pathogenic features of erythrocyte invasion and cytoadherence in malaria are reliant on Plasmodium-specific Duffy-binding-like domains (DBLs). These cysteine-rich modules recognize diverse host cell-surface receptors during pathogenesis. DBLs of parasite erythrocyte-binding proteins mediate invasion, and those from the antigenically variant P. falciparum erythrocyte membrane protein 1 (PfEMP1) have been implicated in cytoadherence. The simian and human malarial parasites, P. knowlesi and P. vivax, invade human erythrocytes exclusively through the host DARC receptor (Duffy antigen receptor for chemokines). Here we present the crystal structure of the P. knowlesi DBL domain (Pkalpha-DBL), which binds to DARC during invasion of human erythrocytes. Pkalpha-DBL retains the overall fold observed in DBLs from P. falciparum erythrocyte-binding antigen (EBA)-175 (ref. 4). Mapping the residues that have previously been implicated in binding highlights a fairly flat but exposed site for DARC recognition in subdomain 2 of Pkalpha-DBL; this is in sharp contrast to receptor recognition by EBA-175 (ref. 4). In Pkalpha-DBL, the residues that contact DARC and the clusters of residues under immune pressure map to opposite surfaces of the DBL, and suggest a possible mechanism for immune evasion by P. vivax. Our comparative structural analysis of Pkalpha-DBL and P. falciparum EBA-175 provides a framework for the understanding of malaria parasite DBLs, and may affect the development of new prophylactic and therapeutic strategies. Structural basis for Duffy recognition by the malaria parasite Duffy-binding-like domain.,Singh SK, Hora R, Belrhali H, Chitnis CE, Sharma A Nature. 2006 Feb 9;439(7077):741-4. Epub 2005 Dec 21. PMID:16372020 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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