2l8s: Difference between revisions
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l8s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l8s RCSB], [http://www.ebi.ac.uk/pdbsum/2l8s PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l8s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l8s RCSB], [http://www.ebi.ac.uk/pdbsum/2l8s PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/ITA1_HUMAN 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. | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 00:21, 25 December 2014
Solution NMR Structure of Transmembrane and Cytosolic Regions of Integrin Alpha1 in Detergent MicellesSolution NMR Structure of Transmembrane and Cytosolic Regions of Integrin Alpha1 in Detergent Micelles
Structural highlights
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 PubMedIntegrin 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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