2l8s

Solution NMR Structure of Transmembrane and Cytosolic Regions of Integrin Alpha1 in Detergent Micelles

spinqualitylabelsall models 2l8s Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l8s is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ITA1_HUMAN Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Publication Abstract from PubMed Integrin proteins are very important adhesion receptors that mediate cell-cell and cell-extracellular matrix interactions. They play essential roles in cell signaling and the regulation of cellular shape, motility, and the cell cycle. Here, the transmembrane and cytoplasmic (TMC) domains of integrin alpha1 and beta1 were over-expressed and purified in detergent micelles. The structure and backbone relaxations of alpha1-TMC in LDAO micelles were determined and analyzed using solution NMR. A long helix, extending from the transmembrane region to the cytoplasmic tail, was observed in alpha1-TMC. Structural comparisons of alpha1-TMC with reported alphaIIb-TMC domains indicated different conformations in the transmembrane regions and cytoplasmic tails. An NMR titration experiment indicated weak interactions between alpha1-TMC and beta1-TMC through several alpha1-TMC residues located at its N-terminal juxta-transmembrane region and C-terminal extended helix region. Integrin alpha1 Has a Long Helix, Extending from the Transmembrane Region to the Cytoplasmic Tail in Detergent Micelles.,Lai C, Liu X, Tian C, Wu F PLoS One. 2013 Apr 30;8(4):e62954. doi: 10.1371/journal.pone.0062954. Print 2013. PMID:23646163 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Integrin 3D structures

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