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J. Biol. Chem., Vol. 283, Issue 23, 16162-16168, June 6, 2008

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Structure of the Integrin IIb Transmembrane Segment^*

From the Department of Biochemistry and Molecular Biology and Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, Los Angeles, California 90033

Integrin cell-adhesion receptors transduce signals bidirectionally across the plasma membrane via the single-pass transmembrane segments of each and β subunit. While the β3 transmembrane segment consists of a linear 29-residue -helix, the structure of the IIb transmembrane segment reveals a linear 24-residue -helix (Ile-966 -Lys-989) followed by a backbone reversal that packs Phe-992-Phe-993 against the transmembrane helix. The length of the IIb transmembrane helix implies the absence of a significant transmembrane helix tilt in contrast to its partnering β3 subunit. Sequence alignment shows Gly-991-Phe-993 to be fully conserved among all 18 human integrin subunits, suggesting that their unusual structural motif is prototypical for integrin subunits. The IIb 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 IIb-β3 association, i.e. integrin transmembrane signaling.

Received for publication, March 4, 2008 , and in revised form, April 10, 2008.

The atomic coordinates and structure factors (code 2k1a) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by an award from the American Heart Association (to T. S. U.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains two supplemental tables and five supplemental figures.

¹ The recipient of a postdoctoral fellowship from the American Heart Association.

² To whom correspondence should be addressed: 1501 San Pablo St., ZNI 111, Los Angeles, CA 90033. Tel.: 323-442-4326; Fax: 323-442-4404; E-mail: tulmer{at}usc.edu.

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