1W81

Crystal structure of apical membrane antigen 1 from Plasmodium vivax

Summary for 1W81

• Entry DOI: 10.2210/pdb1w81/pdb
• Related: 1W8K
• Descriptor: APICAL MEMBRANE ANTIGEN 1, IMIDAZOLE (3 entities in total)
• Functional Keywords: plasmodium antigen, malaria vaccine candidate, antigen
• Biological source: PLASMODIUM VIVAX
• Total number of polymer chains: 1
• Total formula weight: 51666.13

Authors

Pizarro, J.C.,Vulliez-Le Normand, B.,Chesne-Seck, M.-L.,Kocken, C.H.M.,Thomas, A.W.,Bentley, G.A. (deposition date: 2004-09-15, release date: 2005-03-01, Last modification date: 2024-10-09)

Primary citation

Pizarro, J.C.,Vulliez-Le Normand, B.,Chesne-Seck, M.-L.,Collins, C.,Withers-Martinez, C.,Hackett, F.,Blackman, M.,Faber, B.,Remarque, E.,Kocken, C.H.M.,Thomas, A.W.,Bentley, G.A.
Crystal Structure of the Malaria Vaccine Candidate Apical Membrane Antigen 1
Science, 308:408-, 2005

PubMed Abstract: Apical membrane antigen 1 from Plasmodium is a leading malaria vaccine candidate. The protein is essential for host-cell invasion, but its molecular function is unknown. The crystal structure of the three domains comprising the ectoplasmic region of the antigen from P. vivax, solved at 1.8 angstrom resolution, shows that domains I and II belong to the PAN motif, which defines a superfamily of protein folds implicated in receptor binding. We also mapped the epitope of an invasion-inhibitory monoclonal antibody specific for the P. falciparum ortholog and modeled this to the structure. The location of the epitope and current knowledge on structure-function correlations for PAN domains together suggest a receptor-binding role during invasion in which domain II plays a critical part. These results are likely to aid vaccine and drug design.

PubMed: 15731407
DOI: 10.1126/SCIENCE.1107449

Experimental method

X-RAY DIFFRACTION (2.01 Å)