4KFZ
Crystal structure of LMO2 and anti-LMO2 VH complex
Summary for 4KFZ
| Entry DOI | 10.2210/pdb4kfz/pdb |
| Descriptor | LMO-2, Anti-LMO2 VH, ZINC ION (3 entities in total) |
| Functional Keywords | oncoprotein, t-cell leukemia, proto-oncogene, transcription, developmental protein, lim domain, transcription factor, nucleus |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus (Potential): P25791 |
| Total number of polymer chains | 4 |
| Total formula weight | 63620.93 |
| Authors | Sewell, H.,Tanaka, T.,El Omari, K.,Cruz-Migoni, A.,Mancini, E.J.,Fuentes-Fernandez, N.,Chambers, J.,Rabbitts, T.H. (deposition date: 2013-04-28, release date: 2014-01-22, Last modification date: 2023-09-20) |
| Primary citation | Sewell, H.,Tanaka, T.,Omari, K.E.,Mancini, E.J.,Cruz, A.,Fernandez-Fuentes, N.,Chambers, J.,Rabbitts, T.H. Conformational flexibility of the oncogenic protein LMO2 primes the formation of the multi-protein transcription complex. Sci Rep, 4:3643-3643, 2014 Cited by PubMed Abstract: LMO2 was discovered via chromosomal translocations in T-cell leukaemia and shown normally to be essential for haematopoiesis. LMO2 is made up of two LIM only domains (thus it is a LIM-only protein) and forms a bridge in a multi-protein complex. We have studied the mechanism of formation of this complex using a single domain antibody fragment that inhibits LMO2 by sequestering it in a non-functional form. The crystal structure of LMO2 with this antibody fragment has been solved revealing a conformational difference in the positioning and angle between the two LIM domains compared with its normal binding. This contortion occurs by bending at a central helical region of LMO2. This is a unique mechanism for inhibiting an intracellular protein function and the structural contusion implies a model in which newly synthesized, intrinsically disordered LMO2 binds to a partner protein nucleating further interactions and suggests approaches for therapeutic targeting of LMO2. PubMed: 24407558DOI: 10.1038/srep03643 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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