View source for 7c36


==c-Myc DNA binding protein structure==
<StructureSection load='7c36' size='340' side='right'caption='[[7c36]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7c36]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C36 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7c36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c36 OCA], [https://pdbe.org/7c36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c36 RCSB], [https://www.ebi.ac.uk/pdbsum/7c36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c36 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RBMS1_HUMAN 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.
<div style="background-color:#fffaf0;">
== 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<ref>PMID:33999211</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7c36" style="background-color:#fffaf0;"></div>

==See Also==
*[[C-Myc|C-Myc]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Aggarwal P]]
[[Category: Bhavesh NS]]