1idy: Difference between revisions

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-[[Image:1idy.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1idy", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_1idy|  PDB=1idy  |  SCENE=  }}
-'''STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE'''
+==STRUCTURE OF MYB TRANSFORMING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE==
+<StructureSection load='1idy' size='340' side='right'caption='[[1idy]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1idy]] 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=1IDY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IDY FirstGlance]. <br>
+</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1idy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1idy OCA], [https://pdbe.org/1idy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1idy RCSB], [https://www.ebi.ac.uk/pdbsum/1idy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1idy 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/id/1idy_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1idy ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A 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.
-==Overview==
+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<ref>PMID:8942977</ref>
-A 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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-IDY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDY OCA].
+</div>
+<div class="pdbe-citations 1idy" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/8942977 8942977]
+*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Furukawa K]]
-[[Category: Furukawa, K.]]
+[[Category: Nakamura H]]
-[[Category: Nakamura, H.]]
+[[Category: Oda M]]
-[[Category: Oda, M.]]
-[[Category: Dna-binding protein]]
-[[Category: Protooncogene product]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:53:36 2008''