1mbh

<StructureSection load='1mbh' size='340' side='right' caption='[[1mbh]], [[NMR_Ensembles_of_Models | 50 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1mbh]] 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=1MBH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MBH 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">[[1mbg|1mbg]]</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=1mbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mbh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mbh RCSB], [http://www.ebi.ac.uk/pdbsum/1mbh 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/1mbh_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== 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>

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*[[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]]