2K1A
Bicelle-embedded integrin alpha(IIB) transmembrane segment
Summary for 2K1A
| Entry DOI | 10.2210/pdb2k1a/pdb |
| Descriptor | Integrin alpha-IIb (1 entity in total) |
| Functional Keywords | single-pass transmembrane segment, alternative splicing, calcium, cell adhesion, cleavage on pair of basic residues, disease mutation, glycoprotein, integrin, polymorphism, pyrrolidone carboxylic acid, receptor |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Single-pass type I membrane protein: P08514 |
| Total number of polymer chains | 1 |
| Total formula weight | 4751.83 |
| Authors | Lau, T.-L.,Dua, V.,Ulmer, T.S. (deposition date: 2008-02-25, release date: 2008-04-15, Last modification date: 2024-05-29) |
| Primary citation | Lau, T.L.,Dua, V.,Ulmer, T.S. Structure of the Integrin {alpha}IIb Transmembrane Segment. J.Biol.Chem., 283:16162-16168, 2008 Cited by PubMed Abstract: Integrin cell-adhesion receptors transduce signals bidirectionally across the plasma membrane via the single-pass transmembrane segments of each alpha and beta subunit. While the beta3 transmembrane segment consists of a linear 29-residue alpha-helix, the structure of the alphaIIb transmembrane segment reveals a linear 24-residue alpha-helix (Ile-966 -Lys-989) followed by a backbone reversal that packs Phe-992-Phe-993 against the transmembrane helix. The length of the alphaIIb transmembrane helix implies the absence of a significant transmembrane helix tilt in contrast to its partnering beta3 subunit. Sequence alignment shows Gly-991-Phe-993 to be fully conserved among all 18 human integrin alpha subunits, suggesting that their unusual structural motif is prototypical for integrin alpha subunits. The alphaIIb transmembrane structure demonstrates a level of complexity within the membrane that is beyond simple transmembrane helices and forms the structural basis for assessing the extent of structural and topological rearrangements upon alphaIIb-beta3 association, i.e. integrin transmembrane signaling. PubMed: 18417472DOI: 10.1074/jbc.M801748200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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