5XAU

Crystal structure of integrin binding fragment of laminin-511

Summary for 5XAU

• Entry DOI: 10.2210/pdb5xau/pdb
• Descriptor: Laminin subunit alpha-5, Laminin subunit beta-1, Laminin subunit gamma-1, ... (7 entities in total)
• Functional Keywords: laminin, integrin, extracellular matrix protein, cell adhesion
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 6
• Total formula weight: 184954.37

Authors

Takizawa, M.,Arimori, T.,Kitago, Y.,Takagi, J.,Sekiguchi, K. (deposition date: 2017-03-15, release date: 2017-09-20, Last modification date: 2024-10-16)

Primary citation

Takizawa, M.,Arimori, T.,Taniguchi, Y.,Kitago, Y.,Yamashita, E.,Takagi, J.,Sekiguchi, K.
Mechanistic basis for the recognition of laminin-511 by alpha 6 beta 1 integrin.
Sci Adv, 3:e1701497-e1701497, 2017

PubMed Abstract: Laminins regulate diverse cellular functions through interaction with integrins. Two regions of laminins-three laminin globular domains of the α chain (LG1-3) and the carboxyl-terminal tail of the γ chain (γ-tail)-are required for integrin binding, but it remains unclear how the γ-tail contributes to the binding. We determined the crystal structure of the integrin binding fragment of laminin-511, showing that the γ-tail extends to the bottom face of LG1-3. Electron microscopic imaging combined with biochemical analyses showed that integrin binds to the bottom face of LG1-3 with the γ1-tail apposed to the metal ion-dependent adhesion site (MIDAS) of integrin β1. These findings are consistent with a model in which the γ-tail coordinates the metal ion in the MIDAS through its Glu residue.

PubMed: 28879238
DOI: 10.1126/sciadv.1701497

Experimental method

X-RAY DIFFRACTION (1.8 Å)