PDBsum entry 2l4z

Hydrolase, metal binding protein

PDB id: 2l4z

Contents

Protein chain

121 a.a.

Metals

_ZN ×2

PDB id:

2l4z

Name:

Hydrolase, metal binding protein

Title:

Nmr structure of fusion of ctip (641-685) to lmo4-lim1 (18-82)

Structure:

DNA endonuclease rbbp8,lim domain transcription factor lmo4. Chain: a. Synonym: ctbp-interacting protein,ctip,retinoblastoma-binding protein 8,rbbp-8,retinoblastoma-interacting protein and myosin-like,rim, sporulation in the absence of spo11 protein 2 homolog,sae2,breast tumor autoantigen,lim domain only protein 4,lmo-4. Engineered: yes. Mutation: yes.

Source:

Homo sapiens, mus musculus. Human, mouse. Organism_taxid: 9606, 10090. Gene: rbbp8, ctip, lmo4. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

C.Liew,P.H.Stokes,A.H.Kwan,J.M.Matthews

Key ref:

P.H.Stokes et al. (2013). Structural basis of the interaction of the breast cancer oncogene LMO4 with the tumour suppressor CtIP/RBBP8. J Mol Biol, 425, 1101-1110. PubMed id: 23353824 DOI: 10.1016/j.jmb.2013.01.017

Date:

22-Oct-10 Release date: 26-Oct-11

Protein chain

P61969  (LMO4_MOUSE) -  LIM domain transcription factor LMO4 from Mus musculus

Seq: 165 a.a.

Struc: 121 a.a.*

* PDB and UniProt seqs differ at 17 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.1.-.-

DOI no: 10.1016/j.jmb.2013.01.017

J Mol Biol 425:1101-1110 (2013)

PubMed id: 23353824

Structural basis of the interaction of the breast cancer oncogene LMO4 with the tumour suppressor CtIP/RBBP8.

P.H.Stokes, C.W.Liew, A.H.Kwan, P.Foo, H.E.Barker, A.Djamirze, V.O'Reilly, J.E.Visvader, J.P.Mackay, J.M.Matthews.

ABSTRACT

LIM-only protein 4 (LMO4) is strongly linked to the progression of breast cancer. Although the mechanisms underlying this phenomenon are not well understood, a role is emerging for LMO4 in regulation of the cell cycle. We determined the solution structure of LMO4 in complex with CtIP (C-terminal binding protein interacting protein)/RBBP8, a tumour suppressor protein that is involved in cell cycle progression, DNA repair and transcriptional regulation. Our data reveal that CtIP and the essential LMO cofactor LDB1 (LIM-domain binding protein 1) bind to the same face on LMO4 and cannot simultaneously bind to LMO4. We hypothesise that overexpression of LMO4 may disrupt some of the normal tumour suppressor activities of CtIP, thereby contributing to breast cancer progression.