5MC9

Crystal structure of the heterotrimeric integrin-binding region of laminin-111

Summary for 5MC9

• Entry DOI: 10.2210/pdb5mc9/pdb
• Descriptor: Laminin subunit alpha-1, Laminin subunit beta-1, Laminin subunit gamma-1, ... (5 entities in total)
• Functional Keywords: extracellular matrix, cell adhesion, coiled coil, laminin g-like domain
• Biological source: Mus musculus (Mouse); More
• Cellular location: Secreted, extracellular space, extracellular matrix, basement membrane: P19137 P02469 P02468
• Total number of polymer chains: 3
• Total formula weight: 83161.69

Authors

Pulido, D.,Hohenester, E. (deposition date: 2016-11-09, release date: 2017-02-08, Last modification date: 2024-10-16)

Primary citation

Pulido, D.,Hussain, S.A.,Hohenester, E.
Crystal Structure of the Heterotrimeric Integrin-Binding Region of Laminin-111.
Structure, 25:530-535, 2017

PubMed Abstract: Laminins are cell-adhesive glycoproteins that are essential for basement membrane assembly and function. Integrins are important laminin receptors, but their binding site on the heterotrimeric laminins is poorly defined structurally. We report the crystal structure at 2.13 Å resolution of a minimal integrin-binding fragment of mouse laminin-111, consisting of ∼50 residues of α1β1γ1 coiled coil and the first three laminin G-like (LG) domains of the α1 chain. The LG domains adopt a triangular arrangement, with the C terminus of the coiled coil situated between LG1 and LG2. The critical integrin-binding glutamic acid residue in the γ1 chain tail is surface exposed and predicted to bind to the metal ion-dependent adhesion site in the integrin β1 subunit. Additional contacts to the integrin are likely to be made by the LG1 and LG2 surfaces adjacent to the γ1 chain tail, which are notably conserved and free of obstructing glycans.

PubMed: 28132784
DOI: 10.1016/j.str.2017.01.002

Experimental method

X-RAY DIFFRACTION (2.13 Å)