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Solution structure of an EGF module pair from the Plasmodium falciparum merozoite surface protein 1.

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Morgan WD,Birdsall B,Frenkiel TA,Gradwell MG,Burghaus PA,Syed SE,Uthaipibull C,Holder AA,Feeney J

doi

10.1006/jmbi.1999.2753

keywords:

subject

Has Abstract

pub_date

1999-05-28 00:00:00

pages

113-22

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(99)92753-5

journal_volume

289

pub_type

杂志文章

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