Structural highlights
Function
LAMA5_HUMAN Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Publication Abstract from PubMed
Laminins regulate diverse cellular functions through interaction with integrins. Two regions of laminins-three laminin globular domains of the alpha chain (LG1-3) and the carboxyl-terminal tail of the gamma chain (gamma-tail)-are required for integrin binding, but it remains unclear how the gamma-tail contributes to the binding. We determined the crystal structure of the integrin binding fragment of laminin-511, showing that the gamma-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 gamma1-tail apposed to the metal ion-dependent adhesion site (MIDAS) of integrin beta1. These findings are consistent with a model in which the gamma-tail coordinates the metal ion in the MIDAS through its Glu residue.
Mechanistic basis for the recognition of laminin-511 by alpha6beta1 integrin.,Takizawa M, Arimori T, Taniguchi Y, Kitago Y, Yamashita E, Takagi J, Sekiguchi K Sci Adv. 2017 Sep 1;3(9):e1701497. doi: 10.1126/sciadv.1701497. eCollection 2017 , Sep. PMID:28879238[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Takizawa M, Arimori T, Taniguchi Y, Kitago Y, Yamashita E, Takagi J, Sekiguchi K. Mechanistic basis for the recognition of laminin-511 by alpha6beta1 integrin. Sci Adv. 2017 Sep 1;3(9):e1701497. doi: 10.1126/sciadv.1701497. eCollection 2017 , Sep. PMID:28879238 doi:http://dx.doi.org/10.1126/sciadv.1701497
