7C36

c-Myc DNA binding protein structure

Summary for 7C36

• Entry DOI: 10.2210/pdb7c36/pdb
• Descriptor: RNA-binding motif, single-stranded-interacting protein 1 (1 entity in total)
• Functional Keywords: dna binding, c-myc binding, dna binding protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 18077.69

Authors

Aggarwal, P.,Bhavesh, N.S. (deposition date: 2020-05-11, release date: 2021-05-12, Last modification date: 2024-05-15)

Primary citation

Aggarwal, P.,Bhavesh, N.S.
Hinge like domain motion facilitates human RBMS1 protein binding to proto-oncogene c-myc promoter.
Nucleic Acids Res., 49:5943-5955, 2021

PubMed 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.

PubMed: 33999211
DOI: 10.1093/nar/gkab363

Experimental method

SOLUTION NMR