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Summary: The Structural Context of Disease-causing Mutations in
Gap Junctions*S
Received for publication,June 15, 2006 Published, JBC Papers in Press,July 24, 2006, DOI 10.1074/jbc.M605764200
Sarel J. Fleishman1,2
, Adi D. Sabag§1
, Eran Ophir§
, Karen B. Avraham§
, and Nir Ben-Tal3
From the
Department of Biochemistry, George S. Wise Faculty of Life Sciences, and §
Department of Human Molecular Genetics
and Biochemistry, Sackler School of Medicine, Tel-Aviv University, 69978 Ramat Aviv, Israel
Gap junctions form intercellular channels that mediate met-
abolic and electrical signaling between neighboring cells in a
tissue. Lack of an atomic resolution structure of the gap junction
has made it difficult to identify interactions that stabilize its
transmembrane domain. Using a recently computed model of
this domain, which specifies the locations of each amino acid, we
postulated the existence of several interactions and tested them
experimentally. We introduced mutations within the trans-
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