1CEJ
SOLUTION STRUCTURE OF AN EGF MODULE PAIR FROM THE PLASMODIUM FALCIPARUM MEROZOITE SURFACE PROTEIN 1
Summary for 1CEJ
| Entry DOI | 10.2210/pdb1cej/pdb |
| NMR Information | BMRB: 4437 |
| Descriptor | PROTEIN (MEROZOITE SURFACE PROTEIN 1) (1 entity in total) |
| Functional Keywords | egf-like domain, extracellular, modular protein, surface antigen, malaria vaccine component, surface protein |
| Biological source | Plasmodium falciparum (malaria parasite P. falciparum) |
| Total number of polymer chains | 1 |
| Total formula weight | 10644.70 |
| Authors | Morgan, W.D.,Birdsall, B.,Frenkiel, T.A.,Gradwell, M.G.,Burghaus, P.A.,Syed, S.E.H.,Uthaipibull, C.,Holder, A.A.,Feeney, J. (deposition date: 1999-03-08, release date: 1999-05-28, Last modification date: 2024-11-06) |
| Primary citation | Morgan, W.D.,Birdsall, B.,Frenkiel, T.A.,Gradwell, M.G.,Burghaus, P.A.,Syed, S.E.,Uthaipibull, C.,Holder, A.A.,Feeney, J. Solution structure of an EGF module pair from the Plasmodium falciparum merozoite surface protein 1. J.Mol.Biol., 289:113-122, 1999 Cited by PubMed Abstract: The solution structure of the 96-residue C-terminal fragment of the merozoite surface protein 1 (MSP-1) from Plasmodium falciparum has been determined using nuclear magnetic resonance (NMR) spectroscopic measurements on uniformly13C/15N-labelled protein, efficiently expressed in the methylotrophic yeast Komagataella (Pichia) pastoris. The structure has two domains with epidermal growth factor (EGF)-like folds with a novel domain interface for the EGF domain pair interactions, formed from a cluster of hydrophobic residues. This gives the protein a U-shaped overall structure with the N-terminal proteolytic processing site close to the C-terminal glycosyl phosphatidyl inositol (GPI) membrane anchor site, which is consistent with the involvement of a membrane-bound proteinase in the processing of MSP-1 during erythrocyte invasion. This structure, which is the first protozoan EGF example to be determined, contrasts with the elongated structures seen for EGF-module pairs having shared Ca2+-ligation sites at their interface, as found, for example, in fibrillin-1. Recognition surfaces for antibodies that inhibit processing and invasion, and antibodies that block the binding of these inhibitory antibodies, have been mapped on the three-dimensional structure by considering specific MSP-1 mutants. PubMed: 10339410DOI: 10.1006/jmbi.1999.2753 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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