5mc9

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

spinqualitylabelsall models 5mc9, resolution 2.13Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mc9 is a 3 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.13Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. Publication Abstract from PubMed 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Laminin

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