2MSY
Solution structure of Hox homeodomain
Summary for 2MSY
| Entry DOI | 10.2210/pdb2msy/pdb |
| NMR Information | BMRB: 25142 |
| Descriptor | Homeobox protein Hox-C9 (1 entity in total) |
| Functional Keywords | homeodomain, transcription factor, transcription |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P31274 |
| Total number of polymer chains | 1 |
| Total formula weight | 8677.26 |
| Authors | |
| Primary citation | Kim, H.H.,Park, S.J.,Han, J.H.,Pathak, C.,Cheong, H.K.,Lee, B.J. Structural insight into the interaction between the Hox and HMGB1 and understanding of the HMGB1-enhancing effect of Hox-DNA binding. Biochim.Biophys.Acta, 1854:449-459, 2015 Cited by PubMed Abstract: The Hox DNA binding domain, the homeodomain, plays critical roles in genetic control of development and cell fate determination. The variable regulatory functions of Hox proteins are accomplished by binding to target DNA sequences and collaborating protein partners that includes human high mobility group B1 (HMGB1). To better understand the interaction between Hox and HMGB1 and the facilitation of Hox-DNA binding by HMGB1, we solved the solution structure of the homeodomain of Hox including the N-terminal arm region (Hoxc9DBD hereafter). In addition, the details of the interaction between these two proteins, as well as DNA binding of the Hox-HMGB1 complex, were investigated by NMR, ITC, and EMSA. The results suggest that binding of the HMGB1 A-box to Hoxc9DBD makes the loop-1 (loop preceding helix-2 of Hoxc9DBD) more access to DNA backbone, which facilitate Hox-DNA binding with enhanced affinity. PubMed: 25707357DOI: 10.1016/j.bbapap.2015.02.009 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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