2v0x

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[[Image:2v0x.gif|left|200px]]
 
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{{Structure
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==The dimerization domain of LAP2alpha==
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|PDB= 2v0x |SIZE=350|CAPTION= <scene name='initialview01'>2v0x</scene>, resolution 2.2&Aring;
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<StructureSection load='2v0x' size='340' side='right'caption='[[2v0x]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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<table><tr><td colspan='2'>[[2v0x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V0X FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v0x OCA], [https://pdbe.org/2v0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v0x RCSB], [https://www.ebi.ac.uk/pdbsum/2v0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v0x ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v0x OCA], [http://www.ebi.ac.uk/pdbsum/2v0x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v0x RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/LAP2A_MOUSE LAP2A_MOUSE] May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1 (By similarity).
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<div style="background-color:#fffaf0;">
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'''THE DIMERIZATION DOMAIN OF LAP2ALPHA'''
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== Publication Abstract from PubMed ==
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==Overview==
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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.
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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==About this Structure==
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Structural basis for dimerization of LAP2alpha, a component of the nuclear lamina.,Bradley CM, Jones S, Huang Y, Suzuki Y, Kvaratskhelia M, Hickman AB, Craigie R, Dyda F Structure. 2007 Jun;15(6):643-53. PMID:17562312<ref>PMID:17562312</ref>
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2V0X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0X OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural basis for dimerization of LAP2alpha, a component of the nuclear lamina., Bradley CM, Jones S, Huang Y, Suzuki Y, Kvaratskhelia M, Hickman AB, Craigie R, Dyda F, Structure. 2007 Jun;15(6):643-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17562312 17562312]
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</div>
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<div class="pdbe-citations 2v0x" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Bradley CM]]
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[[Category: Bradley, C M.]]
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[[Category: Craigie R]]
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[[Category: Craigie, R.]]
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[[Category: Dyda F]]
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[[Category: Dyda, F.]]
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[[Category: Hickman AB]]
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[[Category: Hickman, A B.]]
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[[Category: Huang Y]]
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[[Category: Huang, Y.]]
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[[Category: Jones S]]
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[[Category: Jones, S.]]
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[[Category: Kvaratskhelia M]]
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[[Category: Kvaratskhelia, M.]]
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[[Category: Suzuki Y]]
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[[Category: Suzuki, Y.]]
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[[Category: alternative splicing]]
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[[Category: cell cycle]]
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[[Category: chromosomal protein]]
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[[Category: coiled coil]]
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[[Category: dna-binding]]
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[[Category: lamin some]]
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[[Category: lamina-associated polypeptide]]
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[[Category: laminopathy]]
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[[Category: nuclear protein]]
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[[Category: phosphorylation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:07:14 2008''
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Current revision

The dimerization domain of LAP2alpha

PDB ID 2v0x

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