2v0x

From Proteopedia

(Difference between revisions)

Revision as of 10:40, 7 July 2021

The dimerization domain of LAP2alpha

Structural highlights

2v0x is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bradley CM, Jones S, Huang Y, Suzuki Y, Kvaratskhelia M, Hickman AB, Craigie R, Dyda F. Structural basis for dimerization of LAP2alpha, a component of the nuclear lamina. Structure. 2007 Jun;15(6):643-53. PMID:17562312 doi:http://dx.doi.org/S0969-2126(07)00174-8

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v0x"

@@ Line 3: / Line 3: @@
 <StructureSection load='2v0x' size='340' side='right'caption='[[2v0x]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2v0x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V0X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2v0x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2v0x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v0x RCSB], [http://www.ebi.ac.uk/pdbsum/2v0x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v0x ProSAT]</span></td></tr>
+<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>
 </table>
 == Function ==
-[[http://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).
+[[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).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2v0x

From Proteopedia

Revision as of 10:40, 7 July 2021

The dimerization domain of LAP2alpha

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox