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PDBsum entry 1uuj
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Cell division
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PDB id
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1uuj
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The structure of the n-Terminal domain of the product of the lissencephaly gene lis1 and its functional implications.
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Authors
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M.H.Kim,
D.R.Cooper,
A.Oleksy,
Y.Devedjiev,
U.Derewenda,
O.Reiner,
J.Otlewski,
Z.S.Derewenda.
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Ref.
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Structure, 2004,
12,
987-998.
[DOI no: ]
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PubMed id
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Abstract
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Mutations in the Lis1 gene result in lissencephaly (smooth brain), a
debilitating developmental syndrome caused by the impaired ability of
postmitotic neurons to migrate to their correct destination in the cerebral
cortex. Sequence similarities suggest that the LIS1 protein contains a
C-terminal seven-blade beta-propeller domain, while the structure of the
N-terminal fragment includes the LisH (Lis-homology) motif, a pattern found in
over 100 eukaryotic proteins with a hitherto unknown function. We present the
1.75 A resolution crystal structure of the N-terminal domain of mouse LIS1, and
we show that the LisH motif is a novel, thermodynamically very stable
dimerization domain. The structure explains the molecular basis of a low
severity form of lissencephaly.
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Figure 5.
Figure 5. The Coiled-Coil SegmentThe coiled coils of C/D
dimer are shown as helices extending from a surface of the LisH
domain. The hydrophobic residues of the heptad repeats are
shown. Surfaces were generated in GRASP (Nicholls et al., 1991).
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
987-998)
copyright 2004.
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