2L4Z
NMR structure of fusion of CtIP (641-685) to LMO4-LIM1 (18-82)
Summary for 2L4Z
| Entry DOI | 10.2210/pdb2l4z/pdb |
| Related | 1M3V 1RUT |
| NMR Information | BMRB: 17265 |
| Descriptor | DNA endonuclease RBBP8,LIM domain transcription factor LMO4, ZINC ION (2 entities in total) |
| Functional Keywords | lim domain, protein-protein interaction, lim-interaction domain, lmo4, rbbp8/ctip, lim-only protein, hydrolase, metal binding protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 1 |
| Total formula weight | 13350.62 |
| Authors | Liew, C.,Stokes, P.H.,Kwan, A.H.,Matthews, J.M. (deposition date: 2010-10-22, release date: 2011-10-26, Last modification date: 2024-05-29) |
| Primary citation | Stokes, P.H.,Liew, C.W.,Kwan, A.H.,Foo, P.,Barker, H.E.,Djamirze, A.,O'Reilly, V.,Visvader, J.E.,Mackay, J.P.,Matthews, J.M. Structural Basis of the Interaction of the Breast Cancer Oncogene LMO4 with the Tumour Suppressor CtIP/RBBP8. J.Mol.Biol., 425:1101-1110, 2013 Cited by PubMed 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. PubMed: 23353824DOI: 10.1016/j.jmb.2013.01.017 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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