Abstract:
:Structures of intact receptors with single-pass transmembrane domains are essential to understand how extracellular and cytoplasmic domains regulate association and signaling through transmembrane domains. A chemical and computational method to determine structures of the membrane regions of such receptors on the cell surface is developed here and validated with glycophorin A. An integrin heterodimer structure reveals association over most of the lengths of the alpha and beta transmembrane domains and shows that the principles governing association of hetero and homo transmembrane dimers differ. A turn at the Gly of the juxtamembrane GFFKR motif caps the alpha TM helix and brings the two Phe of GFFKR into the alpha/beta interface. A juxtamembrane Lys residue in beta also has an important role in the interface. The structure shows how transmembrane association/dissociation regulates integrin signaling. A joint ectodomain and membrane structure shows that substantial flexibility between the extracellular and TM domains is compatible with TM signaling.
journal_name
Mol Celljournal_title
Molecular cellauthors
Zhu J,Luo BH,Barth P,Schonbrun J,Baker D,Springer TAdoi
10.1016/j.molcel.2009.02.022subject
Has Abstractpub_date
2009-04-24 00:00:00pages
234-49issue
2eissn
1097-2765issn
1097-4164pii
S1097-2765(09)00138-5journal_volume
34pub_type
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