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Structure of Human M-type Phospholipase A2 Receptor Revealed by Cryo-Electron Microscopy.

Abstract：

:M-type phospholipase A2 receptor (M-PLA2R) is a member of the mannose receptor family and known as the receptor of secretory phospholipase A2s. It has also been identified as the major autoantigen of idiopathic membranous nephropathy, one of the most common causes for nephrotic syndrome in adults. Here we determine the structure of human M-PLA2R ectodomain by cryo-electron microscopy. The results show that the ectodomain has high internal flexibility and forms a compact dual-ring-shaped conformation at acidic pH and adopts extended conformations at basic pH. The inter-domain interactions of human M-PLA2R are explored by the binding studies with individual domains, showing the mechanism of the conformational change. In addition, the biochemical data suggest that mouse M-PLA2R recognizes mouse secretory phospholipase A2-G1B only at physiological or basic pH, rather than at acidic pH. These results suggest that the pH-dependent conformational change might play important roles in the functional activities of M-PLA2R such as ligand binding and release, and may also be relevant to the immunogenicity in membranous nephropathy.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Dong Y,Cao L,Tang H,Shi X,He Y

doi

10.1016/j.jmb.2017.10.019

subject

Has Abstract

pub_date

2017-12-08 00:00:00

pages

3825-3835

issue

24

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(17)30501-6

journal_volume

429

pub_type

杂志文章

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