Molecular architecture of a complex between an adhesion protein from the malaria parasite and intracellular adhesion molecule 1

TY - JOUR

T1 - Molecular architecture of a complex between an adhesion protein from the malaria parasite and intracellular adhesion molecule 1

AU - Brown, Alan

AU - Turner, Louise

AU - Christoffersen, Stig

AU - Andrews, Katrina A

AU - Szestak, Tadge

AU - Zhao, Yuguang

AU - Larsen, Sine

AU - Craig, Alister G

AU - Higgins, Matthew K

PY - 2013/2/22

Y1 - 2013/2/22

N2 - Background: PfEMP1 proteins cause Plasmodium falciparum-infected erythrocytes to bind human tissues during malaria. Results: The IT4VAR13 ectodomain is rigid, elongated, and monomeric, presenting a binding site for its ligand, ICAM-1. Conclusion: The IT4VAR13 ectodomain is unlike that of VAR2CSA, a PfEMP1 that adopts a compact structure with multiple domains contributing to ligand binding. Significance: PfEMP1 proteins have evolved diverse architectures to facilitate ligand recognition.

AB - Background: PfEMP1 proteins cause Plasmodium falciparum-infected erythrocytes to bind human tissues during malaria. Results: The IT4VAR13 ectodomain is rigid, elongated, and monomeric, presenting a binding site for its ligand, ICAM-1. Conclusion: The IT4VAR13 ectodomain is unlike that of VAR2CSA, a PfEMP1 that adopts a compact structure with multiple domains contributing to ligand binding. Significance: PfEMP1 proteins have evolved diverse architectures to facilitate ligand recognition.

U2 - 10.1074/jbc.M112.416347

DO - 10.1074/jbc.M112.416347

M3 - Journal article

C2 - 23297413

SN - 0021-9258

VL - 288

SP - 5992

EP - 6003

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 8

ER -