PDBsum entry 2m32

Cell adhesion

PDB id: 2m32

Contents

Protein chains

192 a.a.

23 a.a.

Metals

_MG

PDB id:

2m32

Name:

Cell adhesion

Title:

Alpha-1 integrin i-domain in complex with glogen triple helical peptide

Structure:

Integrin alpha-1. Chain: a. Synonym: cd49 antigen-like family member a, laminin and collagen receptor, vla-1. Engineered: yes. Glogen peptide. Chain: b, c, d. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: itga1. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: synthetically obtained

NMR struc:

10 models

Authors:

Y.Chin,S.Headey,B.Mohanty,P.Mcewan,J.Swarbrick,T.Mulhern,J.Emsley, J.Simpson,M.Scanlon

Key ref:

Y.K.Chin et al. (2013). The structure of integrin α1I domain in complex with a collagen-mimetic peptide. J Biol Chem, 288, 36796-36809. PubMed id: 24187131 DOI: 10.1074/jbc.M113.480251

Date:

07-Jan-13 Release date: 06-Nov-13

Protein chain

P56199  (ITA1_HUMAN) -  Integrin alpha-1 from Homo sapiens

Seq: 1179 a.a.

Struc: 192 a.a.

Protein chains

No UniProt id for this chain

Struc: 22 a.a.

DOI no: 10.1074/jbc.M113.480251

J Biol Chem 288:36796-36809 (2013)

PubMed id: 24187131

The structure of integrin α1I domain in complex with a collagen-mimetic peptide.

Y.K.Chin, S.J.Headey, B.Mohanty, R.Patil, P.A.McEwan, J.D.Swarbrick, T.D.Mulhern, J.Emsley, J.S.Simpson, M.J.Scanlon.

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.