1CEJ

SOLUTION STRUCTURE OF AN EGF MODULE PAIR FROM THE PLASMODIUM FALCIPARUM MEROZOITE SURFACE PROTEIN 1

1CEJ の概要

• エントリーDOI: 10.2210/pdb1cej/pdb
• NMR情報: BMRB: 4437
• 分子名称: PROTEIN (MEROZOITE SURFACE PROTEIN 1) (1 entity in total)
• 機能のキーワード: egf-like domain, extracellular, modular protein, surface antigen, malaria vaccine component, surface protein
• 由来する生物種: Plasmodium falciparum (malaria parasite P. falciparum)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10644.70

構造登録者

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. (登録日: 1999-03-08, 公開日: 1999-05-28, 最終更新日: 2024-11-06)

主引用文献

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

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: 10339410
DOI: 10.1006/jmbi.1999.2753

実験手法

SOLUTION NMR