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PDBsum entry 2v0x
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References listed in PDB file
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Key reference
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Title
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Structural basis for dimerization of lap2alpha, A component of the nuclear lamina.
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Authors
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C.M.Bradley,
S.Jones,
Y.Huang,
Y.Suzuki,
M.Kvaratskhelia,
A.B.Hickman,
R.Craigie,
F.Dyda.
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Ref.
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Structure, 2007,
15,
643-653.
[DOI no: ]
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PubMed id
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Abstract
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Lamina-associated polypeptides (LAPs) are important components of the nuclear
lamina, the dense network of filaments that supports the nuclear envelope and
also extends into the nucleoplasm. The main protein constituents of the nuclear
lamina are the constitutively expressed B-type lamins and the developmentally
regulated A- and C-type lamins. LAP2alpha is the only non-membrane-associated
member of the LAP family. It preferentially binds lamin A/C, has been implicated
in cell-cycle regulation and chromatin organization, and has also been found to
be a component of retroviral preintegration complexes. As an approach to
understanding the role of LAP2alpha in cellular pathways, we have determined the
crystal structure of the C-terminal domain of LAP2alpha, residues 459-693. The
C-terminal domain is dimeric and possesses an extensive four-stranded,
antiparallel coiled coil. The surface involved in binding lamin A/C is proposed
based on results from alanine-scanning mutagenesis and a solid-phase overlay
binding assay.
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Figure 3.
Figure 3. The LAP2α C-Terminal Domain Is Dimeric and
Contains a Four-Stranded Coiled Coil
The six helices,
A–F, are indicated for the orange monomer. In the green
monomer, the loop between the arrows (from Ser544 to Ser556) has
been modeled based on its observed conformation in the orange
monomer.
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Figure 7.
Figure 7. Site-Directed Mutations in the LAP2α C-Terminal
Domain Affect Lamin A/C Binding
Shown in red are the
residues that are compromised in lamin A/C binding when mutated
to Ala; shown in blue are those that have enhanced lamin A/C
binding. The region comprising residues 652–669 is shown in
orange and may form part of the lamin A/C-binding site.
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The above figures are
reprinted
by permission from Cell Press:
Structure
(2007,
15,
643-653)
copyright 2007.
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