9CQI

CRYSTAL STRUCTURE OF GAGA-DOG HSP47(36-418) IN COMPLEX WITH ADNECTIN-44

9CQI の概要

• エントリーDOI: 10.2210/pdb9cqi/pdb
• 分子名称: Serpin H1, anti-HSP47 Adnectin-44 (3 entities in total)
• 機能のキーワード: chaperone, serpin h1
• 由来する生物種: Canis lupus familiaris (dog); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55346.85

構造登録者

Sheriff, S. (登録日: 2024-07-19, 公開日: 2024-10-30, 最終更新日: 2024-11-20)

主引用文献

Kish, K.,Cobell, S.,Szapiel, N.,Yan, C.,Newitt, J.A.,Tredup, J.,Rodrigo, I.,Tomasco, E.,Gao, M.,Marsilio, F.,Haugner, J.,Lipovsek, D.,Deng, B.,Bousquet, P.,Zhang, Y.,Schmidt, H.,Sheriff, S.
Improving the diffraction quality of heat-shock protein 47 crystals.
Acta Crystallogr.,Sect.F, 80:302-313, 2024

PubMed Abstract: Heat-shock protein 47 (HSP47) is a potential target for inhibitors that ameliorate fibrosis by reducing collagen assembly. In an effort to develop a structure-based drug-design system, it was not possible to replicate a previous literature result (PDB entry 4au4) for apo dog HSP47; instead, crystal forms were obtained in which pairs of dog HSP47 molecules interacted through a noncleavable C-terminal His-tag to build up tetramers, all of which had multiple molecules of HSP47 in the asymmetric unit and none of which diffracted as well as the literature precedent. To overcome these difficulties, a two-pronged approach was followed: (i) the His-tag was moved from the C-terminus to the N-terminus and was made cleavable, and (ii) Adnectin (derived from the tenth domain of human fibronectin type III) crystallization chaperones were developed. Both approaches provided well diffracting crystals, but the latter approach yielded crystal forms with only one or two HSP47 complexes per asymmetric unit, which made model building less onerous.

PubMed: 39397789
DOI: 10.1107/S2053230X24009233

実験手法

X-RAY DIFFRACTION (1.941 Å)