6IGO

Crystal structure of myelin protein zero-like protein 1 (MPZL1)

6IGO の概要

• エントリーDOI: 10.2210/pdb6igo/pdb
• 分子名称: Myelin protein zero-like protein 1 (1 entity in total)
• 機能のキーワード: receptor, glycoprotein, transmembrane, immunoglobulin, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 91320.07

構造登録者

Yu, T. (登録日: 2018-09-25, 公開日: 2018-11-28, 最終更新日: 2024-11-13)

主引用文献

Yu, T.,Liang, L.,Zhao, X.,Yin, Y.
Structural and biochemical studies of the extracellular domain of Myelin protein zero-like protein 1
Biochem. Biophys. Res. Commun., 506:883-890, 2018

PubMed Abstract: Myelin protein zero-like protein 1 (MPZL1) is a member of the immunoglobulin superfamily, and is also a receptor of concanavalin A (ConA). MPZL1 is upregulated in hepatocellular carcinoma (HCC) and accelerates migration of HCC cells. However, function of MPZL1 as a receptor of ConA and its role in HCC development are largely unknown. To elucidate the functional basis, we have determined the crystal structure of the extracellular domain of MPZL1 at 2.7 Å resolution. Overall, it folds like a typical immunoglobulin variable-like domain that is much like MPZ. Unexpectedly, we found Asn50 is a unique glycosylation site and the glycosylation mediates its interaction with ConA. Furthermore, we also found that MPZL1 exists as a homodimer in the crystal, in which hydrogen bonds between Ser86 and Val145 play an important role. Our results demonstrate that glycosylation of Asn50 is essential for its function as a receptor of ConA. We propose that dimerization of MPZL1 participates in control of its signal transmission in cell adhesion.

PubMed: 30392906
DOI: 10.1016/j.bbrc.2018.10.161

実験手法

X-RAY DIFFRACTION (2.746 Å)