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1F5F

CRYSTAL STRUCTURE OF THE N-TERMINAL G-DOMAIN OF SHBG IN COMPLEX WITH ZINC

1F5F の概要
エントリーDOI10.2210/pdb1f5f/pdb
関連するPDBエントリー1d2s
分子名称SEX HORMONE-BINDING GLOBULIN, CALCIUM ION, ZINC ION, ... (6 entities in total)
機能のキーワードjellyroll, signaling protein
由来する生物種Homo sapiens (human)
細胞内の位置Secreted : P04278
タンパク質・核酸の鎖数1
化学式量合計23132.05
構造登録者
Avvakumov, V.A.,Muller, Y.A.,Hammond, G.L. (登録日: 2000-06-14, 公開日: 2000-09-06, 最終更新日: 2024-11-13)
主引用文献Avvakumov, G.V.,Muller, Y.A.,Hammond, G.L.
Steroid-binding specificity of human sex hormone-binding globulin is influenced by occupancy of a zinc-binding site.
J.Biol.Chem., 275:25920-25925, 2000
Cited by
PubMed Abstract: One calcium-binding site (site I) and a second poorly defined metal-binding site (site II) have been observed previously within the amino-terminal laminin G-like domain (G domain) of human sex hormone-binding globulin (SHBG). By soaking crystals of this structure in 2.5 mm ZnCl(2), site II and a new metal-binding site (site III) were found to bind Zn(2+). Site II is located close to the steroid-binding site, and Zn(2+) is coordinated by the side chains of His(83) and His(136) and the carboxylate group of Asp(65). In this site, Zn(2+) prevents Asp(65) from interacting with the steroid 17beta-hydroxy group and alters the conformations of His(83) and His(136), as well as a disordered region over the steroid-binding site. Site III is formed by the side chains of His(101) and the carboxylate group of Asp(117), and the distance between them (2.7 A) is increased to 3.7 A in the presence of Zn(2+). The affinity of SHBG for estradiol is reduced in the presence of 0. 1-1 mm Zn(2+), whereas its affinity for androgens is unchanged, and chemically-related metal ions (Cd(2+) and Hg(2+)) have similar but less pronounced effects. This is not observed when Zn(2+) coordination at site II is modified by substituting Gln for His(136). An alteration in the steroid-binding specificity of human SHBG by Zn(2+) occupancy of site II may be relevant in male reproductive tissues where zinc concentrations are very high.
PubMed: 10859323
DOI: 10.1074/jbc.M004484200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.7 Å)
構造検証レポート
Validation report summary of 1f5f
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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