1mbj

<StructureSection load='1mbj' size='340' side='right' caption='[[1mbj]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1mbj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MBJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MBJ FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mbk|1mbk]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mbj OCA], [http://pdbe.org/1mbj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mbj RCSB], [http://www.ebi.ac.uk/pdbsum/1mbj PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/MYB_MOUSE MYB_MOUSE]] Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mb/1mbj_consurf.spt"</scriptWhenChecked>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The DNA-binding domain of c-Myb consists of three imperfect tandem repeats (R1, R2 and R3). The three repeats have similar overall architectures, each containing a helix-turn-helix variation motif. The three conserved tryptophans in each repeat participate in forming a hydrophobic core. Comparison of the three repeat structures indicated that cavities are found in the hydrophobic core of R2, which is thermally unstable. On complexation with DNA, the orientations of R2 and R3 are fixed by tight binding and their conformations are slightly changed. No significant changes occur in the chemical shifts of R1 consistent with its loose interaction with DNA.

Comparison of the free and DNA-complexed forms of the DNA-binding domain from c-Myb.,Ogata K, Morikawa S, Nakamura H, Hojo H, Yoshimura S, Zhang R, Aimoto S, Ametani Y, Hirata Z, Sarai A, et al. Nat Struct Biol. 1995 Apr;2(4):309-20. PMID:7796266<ref>PMID:7796266</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1mbj" style="background-color:#fffaf0;"></div>

*[[Transcriptional activator|Transcriptional activator]]

[[Category: Aimoto, S]]

[[Category: Ametani, Y]]

[[Category: Hirata, Z]]

[[Category: Hojo, H]]

[[Category: Ishii, S]]

[[Category: Morikawa, S]]

[[Category: Nakamura, H]]

[[Category: Nishimura, Y]]

[[Category: Ogata, K]]

[[Category: Sarai, A]]

[[Category: Yoshimura, S]]

[[Category: Zhang, R]]

[[Category: Protooncogene product]]