2L8S

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

Summary for 2L8S

• Entry DOI: 10.2210/pdb2l8s/pdb
• NMR Information: BMRB: 17424
• Descriptor: Integrin alpha-1 (1 entity in total)
• Functional Keywords: integrin alpha1, transmembrane region, detergent micelle, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P56199
• Total number of polymer chains: 1
• Total formula weight: 6343.93

Authors

Lai, C.,Liu, X.,Tian, C. (deposition date: 2011-01-24, release date: 2012-02-01, Last modification date: 2024-05-15)

Primary citation

Lai, C.,Liu, X.,Tian, C.,Wu, F.
Integrin Alpha1 Has a Long Helix, Extending from the Transmembrane Region to the Cytoplasmic Tail in Detergent Micelles
Plos One, 8:e62954-e62954, 2013

PubMed Abstract: 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 α1 and β1 were over-expressed and purified in detergent micelles. The structure and backbone relaxations of α1-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 α1-TMC. Structural comparisons of α1-TMC with reported αIIb-TMC domains indicated different conformations in the transmembrane regions and cytoplasmic tails. An NMR titration experiment indicated weak interactions between α1-TMC and β1-TMC through several α1-TMC residues located at its N-terminal juxta-transmembrane region and C-terminal extended helix region.

PubMed: 23646163
DOI: 10.1371/journal.pone.0062954

Experimental method

SOLUTION NMR