7c36 | pdb_00007c36

c-Myc DNA binding protein structure

spinqualitylabelsall models 7c36, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7c36 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: RBMS1, C2orf12, MSSP, MSSP1, SCR2 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RBMS1_HUMAN] Single-stranded DNA binding protein that interacts with the region upstream of the MYC gene. Binds specifically to the DNA sequence motif 5'-[AT]CT[AT][AT]T-3'. Probably has a role in DNA replication. Publication Abstract from PubMed 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. Hinge like domain motion facilitates human RBMS1 protein binding to proto-oncogene c-myc promoter.,Aggarwal P, Bhavesh NS Nucleic Acids Res. 2021 Jun 4;49(10):5943-5955. doi: 10.1093/nar/gkab363. PMID:33999211 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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