9I5A

Crystal structure of wild type perlecan region 3 construct I876-V1272 construct including one laminin IV-like and four laminin EGF-like domains.

9I5A の概要

• エントリーDOI: 10.2210/pdb9i5a/pdb
• 分子名称: Basement membrane-specific heparan sulfate proteoglycan core protein, SUCCINIC ACID, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: basement membrane proteins; perlecan;laminin iv-like; laminin egf-like domains, structural protein
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 86194.65

構造登録者

Sohail, A.A.,Koski, M.K.,Ruddock, L.R. (登録日: 2025-01-27, 公開日: 2025-04-02, 最終更新日: 2025-05-21)

主引用文献

Sohail, A.A.,Koski, M.K.,Ruddock, L.W.
Structural insights on perlecan and Schwartz-Jampel syndrome.
Matrix Biol., 138:1-7, 2025

PubMed Abstract: Perlecan is an essential multi-domain, disulfide bond rich basement membrane protein. Mutations in perlecan cause Schwartz-Jampel syndrome and dyssegmental dysplasia. While there has been a large body of experimental work reported on perlecan, there is only minimal structural information available to date. There is no prior structural data for region 3 of perlecan in which some Schwartz-Jampel syndrome causing point mutations have been reported. Here, we produce constructs of the disulfide rich region 3 of perlecan along with five mutations previously reported to cause Schwatz-Jampel syndrome. Four of the mutations resulted in decreased yields and thermal stability compared to the wild-type protein. In contrast, the P1019L mutation was produced in good yields and showed higher thermal stability than the wild-type protein. The crystal structures for both the wild-type and P1019L mutation were solved. As expected, both showed laminin IV-like and laminin-type EGF-like domains, with the P1019L mutation resulting in only a minor conformational change in a loop region and no significant changes in regular secondary or tertiary structure.

PubMed: 40118124
DOI: 10.1016/j.matbio.2025.03.002

実験手法

X-RAY DIFFRACTION (2.045 Å)