PDBsum entry 2v0x

Cell cycle

PDB id: 2v0x

Contents

Protein chains

195 a.a.

205 a.a.

Waters ×59

PDB id:

2v0x

Name:

Cell cycle

Title:

The dimerization domain of lap2alpha

Structure:

Lamina-associated polypeptide 2 isoforms alpha/zeta. Chain: a, b. Fragment: dimerization domain, residues 458-692. Synonym: thymopoietin isoforms alpha/zeta, tp alpha/zeta, lamina associated polypeptide 2alpha. Engineered: yes. Mutation: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.20Å R-factor: 0.213 R-free: 0.257

Authors:

C.M.Bradley,S.Jones,Y.Huang,Y.Suzuki,M.Kvaratskhelia,A.B.Hickman, R.Craigie,F.Dyda

Key ref:

C.M.Bradley et al. (2007). Structural basis for dimerization of LAP2alpha, a component of the nuclear lamina. Structure, 15, 643-653. PubMed id: 17562312 DOI: 10.1016/j.str.2007.04.007

Date:

20-May-07 Release date: 26-Jun-07

Protein chain

Q61033  (LAP2A_MOUSE) -  Lamina-associated polypeptide 2, isoforms alpha/zeta from Mus musculus

Seq: 693 a.a.

Struc: 195 a.a.

Protein chain

Q61033  (LAP2A_MOUSE) -  Lamina-associated polypeptide 2, isoforms alpha/zeta from Mus musculus

Seq: 693 a.a.

Struc: 205 a.a.*

* PDB and UniProt seqs differ at 8 residue positions (black crosses)

DOI no: 10.1016/j.str.2007.04.007

Structure 15:643-653 (2007)

PubMed id: 17562312

Structural basis for dimerization of LAP2alpha, a component of the nuclear lamina.

C.M.Bradley, S.Jones, Y.Huang, Y.Suzuki, M.Kvaratskhelia, A.B.Hickman, R.Craigie, F.Dyda.

ABSTRACT

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.

Selected figure(s)

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.

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.

The above figures are reprinted by permission from Cell Press: Structure (2007, 15, 643-653) copyright 2007.

Figures were selected by the author.