4R1B
Crystal Structure of 3D7 strain Plasmodium falciparum AMA1
Summary for 4R1B
Entry DOI | 10.2210/pdb4r1b/pdb |
Related | 4R19 4R1A 4R1C |
Descriptor | Apical membrane antigen 1, AMA1 (2 entities in total) |
Functional Keywords | pan fold, erythrocyte invasion by merozoites, ron2, moving junction complex, cell invasion |
Biological source | Plasmodium falciparum 3D7 |
Total number of polymer chains | 1 |
Total formula weight | 38360.05 |
Authors | Lim, S.S.,Norton, R.S.,McGowan, S. (deposition date: 2014-08-04, release date: 2015-01-14, Last modification date: 2023-09-20) |
Primary citation | Lim, S.S.,Yang, W.,Krishnarjuna, B.,Kannan Sivaraman, K.,Chandrashekaran, I.R.,Kass, I.,MacRaild, C.A.,Devine, S.M.,Debono, C.O.,Anders, R.F.,Scanlon, M.J.,Scammells, P.J.,Norton, R.S.,McGowan, S. Structure and Dynamics of Apical Membrane Antigen 1 from Plasmodium falciparum FVO. Biochemistry, 53:7310-7320, 2014 Cited by PubMed Abstract: Apical membrane antigen 1 (AMA1) interacts with RON2 to form a protein complex that plays a key role in the invasion of host cells by malaria parasites. Blocking this protein-protein interaction represents a potential route to controlling malaria and related parasitic diseases, but the polymorphic nature of AMA1 has proven to be a major challenge to vaccine-induced antibodies and peptide inhibitors exerting strain-transcending inhibitory effects. Here we present the X-ray crystal structure of AMA1 domains I and II from Plasmodium falciparum strain FVO. We compare our new structure to those of AMA1 from P. falciparum 3D7 and Plasmodium vivax. A combination of normalized B factor analysis and computational methods has been used to investigate the flexibility of the domain I loops and how this correlates with their roles in determining the strain specificity of human antibody responses and inhibitory peptides. We also investigated the domain II loop, a key region involved in inhibitor binding, by comparison of multiple AMA1 crystal structures. Collectively, these results provide valuable insights that should contribute to the design of strain-transcending agents targeting P. falciparum AMA1. PubMed: 25360546DOI: 10.1021/bi5012089 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
Download full validation report