5X6N

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

「2C6J」から置き換えられました

5X6N の概要

• エントリーDOI: 10.2210/pdb5x6n/pdb
• 分子名称: Duffy binding protein, octyl beta-D-glucopyranoside, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: receptor, duffy antigen, dbl domain, p.knowlesi, p.vivax, cell invasion
• 由来する生物種: Plasmodium knowlesi
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40390.19

構造登録者

Singh, S.K.,Hora, R.,Belrhali, H.,Chitnis, C.,Sharma, A. (登録日: 2017-02-22, 公開日: 2017-03-08, 最終更新日: 2024-11-20)

主引用文献

Singh, S.K.,Hora, R.,Belrhali, H.,Chitnis, C.E.,Sharma, A.
Structural basis for Duffy recognition by the malaria parasite Duffy-binding-like domain
Nature, 439:741-744, 2006

PubMed Abstract: 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.

PubMed: 16372020
DOI: 10.1038/nature04443

実験手法

X-RAY DIFFRACTION (3 Å)