5KTF

Structure of the C-terminal transmembrane domain of scavenger receptor BI (SR-BI)

5KTF の概要

• エントリーDOI: 10.2210/pdb5ktf/pdb
• NMR情報: BMRB: 30137
• 分子名称: Scavenger receptor class B member 1 (1 entity in total)
• 機能のキーワード: sr-bi, transmembrane domain, cholesterol, signaling protein
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8185.79

構造登録者

Chadwick, A.C.,Peterson, F.C.,Volkman, B.F.,Sahoo, D. (登録日: 2016-07-11, 公開日: 2017-03-08, 最終更新日: 2024-05-15)

主引用文献

Chadwick, A.C.,Jensen, D.R.,Hanson, P.J.,Lange, P.T.,Proudfoot, S.C.,Peterson, F.C.,Volkman, B.F.,Sahoo, D.
NMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif.
Structure, 25:446-457, 2017

PubMed Abstract: The interaction of high-density lipoprotein (HDL) with its receptor, scavenger receptor BI (SR-BI), is critical for lowering plasma cholesterol levels and reducing the risk for cardiovascular disease. The HDL/SR-BI complex facilitates delivery of cholesterol into cells and is likely mediated by receptor dimerization. This work describes the use of nuclear magnetic resonance (NMR) spectroscopy to generate the first high-resolution structure of the C-terminal transmembrane domain of SR-BI. This region of SR-BI harbors a leucine zipper dimerization motif, which when mutated impairs the ability of the receptor to bind HDL and mediate cholesterol delivery. These losses in function correlate with the inability of SR-BI to form dimers. We also identify juxtamembrane regions of the extracellular domain of SR-BI that may interact with the lipid surface to facilitate cholesterol transport functions of the receptor.

PubMed: 28162952
DOI: 10.1016/j.str.2017.01.001

実験手法

SOLUTION NMR