2M32

Alpha-1 integrin I-domain in complex with GLOGEN triple helical peptide

2M32 の概要

• エントリーDOI: 10.2210/pdb2m32/pdb
• NMR情報: BMRB: 18942
• 分子名称: Integrin alpha-1, GLOGEN peptide, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: alpha-1 integrin, i-domain, glogen, 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: P56199
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 27423.82

構造登録者

Chin, Y.,Headey, S.,Mohanty, B.,McEwan, P.,Swarbrick, J.,Mulhern, T.,Emsley, J.,Simpson, J.,Scanlon, M. (登録日: 2013-01-07, 公開日: 2013-11-06, 最終更新日: 2014-02-12)

主引用文献

Chin, Y.K.,Headey, S.J.,Mohanty, B.,Patil, R.,McEwan, P.A.,Swarbrick, J.D.,Mulhern, T.D.,Emsley, J.,Simpson, J.S.,Scanlon, M.J.
The Structure of Integrin alpha 1I Domain in Complex with a Collagen-mimetic Peptide.
J.Biol.Chem., 288:36796-36809, 2013

PubMed Abstract: We have determined the structure of the human integrin α1I domain bound to a triple-helical collagen peptide. The structure of the α1I-peptide complex was investigated using data from NMR, small angle x-ray scattering, and size exclusion chromatography that were used to generate and validate a model of the complex using the data-driven docking program, HADDOCK (High Ambiguity Driven Biomolecular Docking). The structure revealed that the α1I domain undergoes a major conformational change upon binding of the collagen peptide. This involves a large movement in the C-terminal helix of the αI domain that has been suggested to be the mechanism by which signals are propagated in the intact integrin receptor. The structure suggests a basis for the different binding selectivity observed for the α1I and α2I domains. Mutational data identify residues that contribute to the conformational change observed. Furthermore, small angle x-ray scattering data suggest that at low collagen peptide concentrations the complex exists in equilibrium between a 1:1 and 2:1 α1I-peptide complex.

PubMed: 24187131
DOI: 10.1074/jbc.M113.480251

実験手法

SOLUTION NMR