PDBsum entry: 2jqd

Gene regulation, protein binding

PDB id: 2jqd

Contents

Protein chain

164 a.a. *

* Residue conservation analysis

PDB id:

2jqd

Name:

Gene regulation, protein binding

Title:

Structure of the leucine-rich repeat domain of lanp

Structure:

Acidic leucine-rich nuclear phosphoprotein 32 family member a. Chain: a. Fragment: the n-terminal lrr domain of lanp. Synonym: potent heat-stable protein phosphatase 2a inhibitor i1pp2a, acidic nuclear phosphoprotein pp32, leucine-rich acidic nuclear protein, phapi, mapm. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Gene: anp32a, anp32, lanp. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: de3.

NMR struc:

10 models

Authors:

C.De Chiara,A.Pastore

Key ref:

C.de Chiara et al. (2008). Structural bases for recognition of Anp32/LANP proteins. Febs J, 275, 2548-2560. PubMed id: 18410380 DOI: 10.1111/j.1742-4658.2008.06403.x

Date:

31-May-07 Release date: 22-Apr-08

Protein chain

O35381  (AN32A_MOUSE) -  Acidic leucine-rich nuclear phosphoprotein 32 family member A

Seq: 247 a.a.

Struc: 164 a.a.

 Gene Ontology (GO) functional annotation 

• Biochemical function: protein binding (1 term)

DOI no: 10.1111/j.1742-4658.2008.06403.x

Febs J 275:2548-2560 (2008)

PubMed id: 18410380

Structural bases for recognition of Anp32/LANP proteins.

C.de Chiara, R.P.Menon, A.Pastore.

ABSTRACT

The leucine-rich repeat acidic nuclear protein (Anp32a/LANP) belongs to a family of evolutionarily-conserved phosphoproteins involved in a complex network of protein-protein interactions. In an effort to understand the cellular role, we have investigated the mode of interaction of Anp32a with its partners. As a prerequisite, we solved the structure in solution of the evolutionarily conserved N-terminal leucine-rich repeat (LRR) domain and modeled its interactions with other proteins, taking PP2A as a paradigmatic example. The interaction between the Anp32a LRR domain and the AXH domain of ataxin-1 was probed experimentally. The two isolated and unmodified domains bind with very weak (millimolar) affinity, thus suggesting the necessity either for an additional partner (e.g. other regions of either or both proteins or a third molecule) or for a post-translational modification. Finally, we identified by two-hybrid screening a new partner of the LRR domain, i.e. the microtubule plus-end tracking protein Clip 170/Restin, known to regulate the dynamic properties of microtubules and to be associated with severe human pathologies.