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New page: left|200px<br /><applet load="1mbf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mbf" /> '''MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 1'''<b... |
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== | ==MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 1== | ||
The DNA-binding domain of c-Myb consists of three imperfect tandem repeats | <StructureSection load='1mbf' size='340' side='right'caption='[[1mbf]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1mbf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MBF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MBF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 50 models</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=1mbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mbf OCA], [https://pdbe.org/1mbf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mbf RCSB], [https://www.ebi.ac.uk/pdbsum/1mbf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mbf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mb/1mbf_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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/main_output.php?pdb_ID=1mbf ConSurf]. | |||
<div style="clear:both"></div> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1mbf" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Aimoto S]] | |||
[[Category: Aimoto | [[Category: Ametani Y]] | ||
[[Category: Ametani | [[Category: Hirata Z]] | ||
[[Category: Hirata | [[Category: Hojo H]] | ||
[[Category: Hojo | [[Category: Ishii S]] | ||
[[Category: Ishii | [[Category: Morikawa S]] | ||
[[Category: Morikawa | [[Category: Nakamura H]] | ||
[[Category: Nakamura | [[Category: Nishimura Y]] | ||
[[Category: Nishimura | [[Category: Ogata K]] | ||
[[Category: Ogata | [[Category: Sarai A]] | ||
[[Category: Sarai | [[Category: Yoshimura S]] | ||
[[Category: Yoshimura | [[Category: Zhang R]] | ||
[[Category: Zhang | |||
Latest revision as of 07:43, 17 October 2024
MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 1MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 1
Structural highlights
FunctionMYB_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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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