2N9Y

Structure of the Integrin alphaIIb-beta3(A711P) Transmembrane Complex

2N9Y の概要

• エントリーDOI: 10.2210/pdb2n9y/pdb
• 関連するPDBエントリー: 2K9J
• NMR情報: BMRB: 25920
• 分子名称: Integrin alpha-IIb, Integrin beta-3 (2 entities in total)
• 機能のキーワード: transmembrane complex, integrin receptor, cell adhesion, helix kink, membrane protein-cell adhesion complex, membrane protein/cell adhesion
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P08514; Cell membrane ; Single- pass type I membrane protein : P05106
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 9528.75

構造登録者

Schmidt, T.,Situ, A.J.,Ulmer, T.S. (登録日: 2015-12-14, 公開日: 2016-08-03, 最終更新日: 2024-11-06)

主引用文献

Schmidt, T.,Situ, A.J.,Ulmer, T.S.
Structural and thermodynamic basis of proline-induced transmembrane complex stabilization.
Sci Rep, 6:29809-29809, 2016

PubMed Abstract: In membrane proteins, proline-mediated helix kinks are indispensable for the tight packing of transmembrane (TM) helices. However, kinks invariably affect numerous interhelical interactions, questioning the acceptance of proline substitutions and evolutionary origin of kinks. Here, we present the structural and thermodynamic basis of proline-induced integrin αIIbβ3 TM complex stabilization to understand the introduction of proline kinks in membrane proteins. In phospholipid bicelles, the A711P substitution in the center of the β3 TM helix changes the direction of adjacent helix segments to form a 35 ± 2° angle and predominantly repacks the segment in the inner membrane leaflet due to a swivel movement. This swivel repacks hydrophobic and electrostatic interhelical contacts within intracellular lipids, resulting in an overall TM complex stabilization of -0.82 ± 0.01 kcal/mol. Thus, proline substitutions can directly stabilize membrane proteins and such substitutions are proposed to follow the structural template of integrin αIIbβ3(A711P).

PubMed: 27436065
DOI: 10.1038/srep29809

実験手法

SOLUTION NMR