Abstract:
:We have characterized a membrane protein containing residues P688-T762 of the integrin beta3 subunit, encompassing its transmembrane and cytoplasmic domains, by nuclear magnetic resonance spectroscopy. Under conditions in which it is monomeric in dodecylphosphocholine micelles, the protein consists mainly of alpha-helical structures. An amino-terminal helix corresponding to the beta3 transmembrane helix extends into the membrane-proximal region of the cytoplasmic domain. Moreover, following an apparent hinge at residues H722-D723, residues K725-A735 are mostly alpha-helical. In the presence of membrane-mimicking detergents, the cytoplasmic domain connected to the transmembrane helix is substantially ordered at pH 4.8 and 50 degrees C. Its carboxyl-terminal end takes on a turn-helix configuration characteristic of the immunoreceptor tyrosine-based activation motif. These structural features of the beta3 subunit should help to explain its interaction with numerous cytosolic interacting proteins and begin to illuminate the mechanism of integrin activation.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Li R,Babu CR,Valentine K,Lear JD,Wand AJ,Bennett JS,DeGrado WFdoi
10.1021/bi026822lsubject
Has Abstractpub_date
2002-12-31 00:00:00pages
15618-24issue
52eissn
0006-2960issn
1520-4995pii
bi026822ljournal_volume
41pub_type
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