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PDBsum entry 3j41
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Transport protein/calcium binding
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PDB id
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3j41
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References listed in PDB file
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Key reference
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Title
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Allosteric mechanism of water-Channel gating by ca2+-Calmodulin.
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Authors
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S.L.Reichow,
D.M.Clemens,
J.A.Freites,
K.L.Németh-Cahalan,
M.Heyden,
D.J.Tobias,
J.E.Hall,
T.Gonen.
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Ref.
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Nat Struct Biol, 2013,
20,
1085-1092.
[DOI no: ]
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PubMed id
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Abstract
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Calmodulin (CaM) is a universal regulatory protein that communicates the
presence of calcium to its molecular targets and correspondingly modulates their
function. This key signaling protein is important for controlling the activity
of hundreds of membrane channels and transporters. However, understanding of the
structural mechanisms driving CaM regulation of full-length membrane proteins
has remained elusive. In this study, we determined the pseudoatomic structure of
full-length mammalian aquaporin-0 (AQP0, Bos taurus) in complex with CaM, using
EM to elucidate how this signaling protein modulates water-channel function.
Molecular dynamics and functional mutation studies reveal how CaM binding
inhibits AQP0 water permeability by allosterically closing the cytoplasmic gate
of AQP0. Our mechanistic model provides new insight, only possible in the
context of the fully assembled channel, into how CaM regulates multimeric
channels by facilitating cooperativity between adjacent subunits.
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