Summary information and primary citation
- PDB-id
- 6m75; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- DNA binding protein-DNA
- Method
- X-ray (2.57 Å)
- Summary
- C-myc DNA binding protein complex
- Reference
- Aggarwal P, Bhavesh NS (2021): "Hinge like domain motion facilitates human RBMS1 protein binding to proto-oncogene c-myc promoter." Nucleic Acids Res., 49, 5943-5955. doi: 10.1093/nar/gkab363.
- Abstract
- DNA binding proteins recognize DNA specifically or non-specifically using direct and indirect readout mechanisms like sliding, hopping, and diffusion. However, a common difficulty in explicitly elucidating any particular mechanism of site-specific DNA-protein recognition is the lack of knowledge regarding target sequences and inadequate account of non-specific interactions, in general. Here, we decipher the structural basis of target search performed by the key regulator of expression of c-myc proto-oncogene, the human RBMS1 protein. In this study, we have shown the structural reorganization of this multi-domain protein required for recognizing the specific c-myc promoter sequence. The results suggest that a synergy between structural re-organization and thermodynamics is necessary for the recognition of target sequences. The study presents another perspective of looking at the DNA-protein interactions.