1idz: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='1idz' size='340' side='right'caption='[[1idz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1idz' size='340' side='right'caption='[[1idz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1idz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDZ OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[1idz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IDZ FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1idy|1idy]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1idy|1idy]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1idz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1idz OCA], [https://pdbe.org/1idz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1idz RCSB], [https://www.ebi.ac.uk/pdbsum/1idz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1idz 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 30: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[Transcriptional activator|Transcriptional activator]] | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:40, 7 April 2021
STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, 20 STRUCTURESSTRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, 20 STRUCTURES
Structural highlights
Function[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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA small globular protein, the third repeat of the c-Myb DNA-binding domain, which is composed of 54 amino acid residues, was engineered so as to understand the structural uniqueness of native proteins. This small protein has three alpha-helices that form a helix-turn-helix structure, which is maintained by the hydrophobic core with three Ile residues. One of the mutant proteins, with two of the buried Ile (Ile-155 and Ile-181) substituted with Leu residues, showed multiple conformations, as monitored by heteronuclear magnetic resonance spectroscopy for 13C- and 15N-labeled proteins. The increase in the side-chain conformational entropy, caused by changing the Ile to a Leu residue on an alpha-helix, could engender the lack of structural uniqueness. In native proteins, the conformations of not only the beta-branched side chains, but also those of the neighboring bulky side chains, can be greatly restricted, depending upon the local backbone structure. A small engineered protein lacks structural uniqueness by increasing the side-chain conformational entropy.,Furukawa K, Oda M, Nakamura H Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13583-8. PMID:8942977[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||