1mbj
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 3== | ==MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 3== | ||
| - | <StructureSection load='1mbj' size='340' side='right'caption='[[1mbj | + | <StructureSection load='1mbj' size='340' side='right'caption='[[1mbj]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mbj]] 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=1MBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MBJ FirstGlance]. <br> | <table><tr><td colspan='2'>[[1mbj]] 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=1MBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MBJ FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id=' | + | <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=1mbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mbj OCA], [https://pdbe.org/1mbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mbj RCSB], [https://www.ebi.ac.uk/pdbsum/1mbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mbj ProSAT]</span></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=1mbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mbj OCA], [https://pdbe.org/1mbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mbj RCSB], [https://www.ebi.ac.uk/pdbsum/1mbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mbj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 20: | Line 20: | ||
</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=1mbj ConSurf]. | </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=1mbj ConSurf]. | ||
<div style="clear:both"></div> | <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 1mbj" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Aimoto | + | [[Category: Aimoto S]] |
| - | [[Category: Ametani | + | [[Category: Ametani Y]] |
| - | [[Category: Hirata | + | [[Category: Hirata Z]] |
| - | [[Category: Hojo | + | [[Category: Hojo H]] |
| - | [[Category: Ishii | + | [[Category: Ishii S]] |
| - | [[Category: Morikawa | + | [[Category: Morikawa S]] |
| - | [[Category: Nakamura | + | [[Category: Nakamura H]] |
| - | [[Category: Nishimura | + | [[Category: Nishimura Y]] |
| - | [[Category: Ogata | + | [[Category: Ogata K]] |
| - | [[Category: Sarai | + | [[Category: Sarai A]] |
| - | [[Category: Yoshimura | + | [[Category: Yoshimura S]] |
| - | [[Category: Zhang | + | [[Category: Zhang R]] |
| - | + | ||
| - | + | ||
Revision as of 08:33, 10 April 2024
MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 3
| |||||||||||
Categories: Large Structures | Mus musculus | Aimoto S | Ametani Y | Hirata Z | Hojo H | Ishii S | Morikawa S | Nakamura H | Nishimura Y | Ogata K | Sarai A | Yoshimura S | Zhang R
