4BJ3

Integrin alpha2 I domain E318W-collagen complex

Summary for 4BJ3

• Entry DOI: 10.2210/pdb4bj3/pdb
• Descriptor: INTEGRIN ALPHA-2, GFOGER PEPTIDE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: cell adhesion
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Membrane; Single-pass type I membrane protein: P17301
• Total number of polymer chains: 5
• Total formula weight: 56613.46

Authors

Carafoli, F.,Hamaia, S.W.,Bihan, D.,Hohenester, E.,Farndale, R.W. (deposition date: 2013-04-16, release date: 2013-11-20, Last modification date: 2023-12-20)

Primary citation

Carafoli, F.,Hamaia, S.W.,Bihan, D.,Hohenester, E.,Farndale, R.W.
An Activating Mutation Reveals a Second Binding Mode of the Integrin Alpha2 I Domain to the Gfoger Motif in Collagens.
Plos One, 8:69833-, 2013

PubMed Abstract: The GFOGER motif in collagens (O denotes hydroxyproline) represents a high-affinity binding site for all collagen-binding integrins. Other GxOGER motifs require integrin activation for maximal binding. The E318W mutant of the integrin α2β1 I domain displays a relaxed collagen specificity, typical of an active state. E318W binds more strongly than the wild-type α2 I domain to GMOGER, and forms a 2:1 complex with a homotrimeric, collagen-like, GFOGER peptide. Crystal structure analysis of this complex reveals two E318W I domains, A and B, bound to a single triple helix. The E318W I domains are virtually identical to the collagen-bound wild-type I domain, suggesting that the E318W mutation activates the I domain by destabilising the unligated conformation. E318W I domain A interacts with two collagen chains similarly to wild-type I domain (high-affinity mode). E318W I domain B makes favourable interactions with only one collagen chain (low-affinity mode). This observation suggests that single GxOGER motifs in the heterotrimeric collagens V and IX may support binding of activated integrins.

PubMed: 23922814
DOI: 10.1371/JOURNAL.PONE.0069833

Experimental method

X-RAY DIFFRACTION (3.042 Å)