5mc9
From Proteopedia
Crystal structure of the heterotrimeric integrin-binding region of laminin-111
Structural highlights
Function[LAMA1_MOUSE] 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. [LAMC1_MOUSE] 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. [LAMB1_MOUSE] 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. Involved in the organization of the laminar architecture of the cerebral cortex (By similarity). It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons (By similarity). Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface (By similarity). Publication Abstract from PubMedLaminins 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 A resolution of a minimal integrin-binding fragment of mouse laminin-111, consisting of approximately 50 residues of alpha1beta1gamma1 coiled coil and the first three laminin G-like (LG) domains of the alpha1 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 gamma1 chain tail is surface exposed and predicted to bind to the metal ion-dependent adhesion site in the integrin beta1 subunit. Additional contacts to the integrin are likely to be made by the LG1 and LG2 surfaces adjacent to the gamma1 chain tail, which are notably conserved and free of obstructing glycans. Crystal Structure of the Heterotrimeric Integrin-Binding Region of Laminin-111.,Pulido D, Hussain SA, Hohenester E Structure. 2017 Mar 7;25(3):530-535. doi: 10.1016/j.str.2017.01.002. Epub 2017, Jan 26. PMID:28132784[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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