2L8S

Solution NMR Structure of Transmembrane and Cytosolic Regions of Integrin Alpha1 in Detergent Micelles

2L8S の概要

• エントリーDOI: 10.2210/pdb2l8s/pdb
• NMR情報: BMRB: 17424
• 分子名称: Integrin alpha-1 (1 entity in total)
• 機能のキーワード: integrin alpha1, transmembrane region, detergent micelle, cell adhesion
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P56199
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6343.93

構造登録者

Lai, C.,Liu, X.,Tian, C. (登録日: 2011-01-24, 公開日: 2012-02-01, 最終更新日: 2024-05-15)

主引用文献

Lai, C.,Liu, X.,Tian, C.,Wu, F.
Integrin Alpha1 Has a Long Helix, Extending from the Transmembrane Region to the Cytoplasmic Tail in Detergent Micelles
Plos One, 8:e62954-e62954, 2013

PubMed Abstract: Integrin proteins are very important adhesion receptors that mediate cell-cell and cell-extracellular matrix interactions. They play essential roles in cell signaling and the regulation of cellular shape, motility, and the cell cycle. Here, the transmembrane and cytoplasmic (TMC) domains of integrin α1 and β1 were over-expressed and purified in detergent micelles. The structure and backbone relaxations of α1-TMC in LDAO micelles were determined and analyzed using solution NMR. A long helix, extending from the transmembrane region to the cytoplasmic tail, was observed in α1-TMC. Structural comparisons of α1-TMC with reported αIIb-TMC domains indicated different conformations in the transmembrane regions and cytoplasmic tails. An NMR titration experiment indicated weak interactions between α1-TMC and β1-TMC through several α1-TMC residues located at its N-terminal juxta-transmembrane region and C-terminal extended helix region.

PubMed: 23646163
DOI: 10.1371/journal.pone.0062954

実験手法

SOLUTION NMR