6ZBL

Plasmodium falciparum merozoite surface protein 1 dimer, conformation 2

6ZBL の概要

• エントリーDOI: 10.2210/pdb6zbl/pdb
• 関連するPDBエントリー: 6ZBC 6ZBD 6ZBE 6ZBF 6ZBG 6ZBH 6ZBJ
• EMDBエントリー: 11150 11151 11152 11153 11154 11155 11156 11157
• 分子名称: Precursor of the major merozoite surface antigens, Merozoite surface protein-1 (2 entities in total)
• 機能のキーワード: merozoite surface protein 1, malaria, plasmodium falciparum, msp-1, p190, gpi-anchored membrane protein, membrane protein
• 由来する生物種: Plasmodium falciparum; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 383177.95

構造登録者

Dijkman, P.M.,Kudryashev, M. (登録日: 2020-06-08, 公開日: 2021-05-19, 最終更新日: 2024-11-06)

主引用文献

Dijkman, P.M.,Marzluf, T.,Zhang, Y.,Chang, S.S.,Helm, D.,Lanzer, M.,Bujard, H.,Kudryashev, M.
Structure of the merozoite surface protein 1 from Plasmodium falciparum .
Sci Adv, 7:-, 2021

PubMed Abstract: The merozoite surface protein 1 (MSP-1) is the most abundant protein on the surface of the erythrocyte-invading merozoite, the causative agent of malaria. MSP-1 is essential for merozoite formation, entry into and escape from erythrocytes, and is a promising vaccine candidate. Here, we present monomeric and dimeric structures of full-length MSP-1. MSP-1 adopts an unusual fold with a large central cavity. Its fold includes several coiled-coils and shows structural homology to proteins associated with membrane and cytoskeleton interactions. MSP-1 formed dimers through these domains in a concentration-dependent manner. Dimerization is affected by the presence of the erythrocyte cytoskeleton protein spectrin, which may compete for the dimerization interface. Our work provides structural insights into the possible mode of interaction of MSP-1 with erythrocytes and establishes a framework for future investigations into the role of MSP-1 in infection and immunity.

PubMed: 34078606
DOI: 10.1126/sciadv.abg0465

実験手法

ELECTRON MICROSCOPY (3.6 Å)