1mdy: Difference between revisions

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New page: left|200px<br /><applet load="1mdy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mdy, resolution 2.800Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1mdy.gif|left|200px]]<br /><applet load="1mdy" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1mdy, resolution 2.800&Aring;" />
'''CRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION'''<br />


==Overview==
==CRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION==
The crystal structure of a MyoD basic-helix-loop-helix (bHLH) domain-DNA, complex has been solved and refined at 2.8 A resolution. This structure, proves that bHLH and bHLH-leucine zipper (bHLH-ZIP) proteins are, remarkably similar; it helps us understand subtle differences in binding, preferences for these proteins; and it has surprising implications for our, understanding of transcription. Specifically, Ala-114 and Thr-115, which, are required for positive control in the myogenic proteins, are buried at, the protein-DNA interface. These residues are not available for direct, protein-protein contacts, but they may determine the conformation of, Arg-111. Comparisons with Max suggest that the conformation of this, arginine, which is different in the two structures, may play an important, role in myogenic transcription.
<StructureSection load='1mdy' size='340' side='right'caption='[[1mdy]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1mdy]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MDY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MDY FirstGlance]. <br>
1MDY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MDY OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=1mdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mdy OCA], [https://pdbe.org/1mdy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mdy RCSB], [https://www.ebi.ac.uk/pdbsum/1mdy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mdy ProSAT]</span></td></tr>
==Reference==
</table>
Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation., Ma PC, Rould MA, Weintraub H, Pabo CO, Cell. 1994 May 6;77(3):451-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8181063 8181063]
== Function ==
[https://www.uniprot.org/uniprot/MYOD1_MOUSE MYOD1_MOUSE] Involved in muscle differentiation (myogenic factor). Induces fibroblasts to differentiate into myoblasts. Activates muscle-specific promoters. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins.<ref>PMID:3175662</ref>
== 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/md/1mdy_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=1mdy ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Ma PCM]]
[[Category: Ma, P.C.M.]]
[[Category: Pabo CO]]
[[Category: Pabo, C.O.]]
[[Category: Rould MA]]
[[Category: Rould, M.A.]]
[[Category: Weintraub H]]
[[Category: Weintraub, H.]]
[[Category: protein-dna complex]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:21:20 2007''

Latest revision as of 10:43, 14 February 2024

CRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATIONCRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION

Structural highlights

1mdy is a 8 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYOD1_MOUSE Involved in muscle differentiation (myogenic factor). Induces fibroblasts to differentiate into myoblasts. Activates muscle-specific promoters. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Tapscott SJ, Davis RL, Thayer MJ, Cheng PF, Weintraub H, Lassar AB. MyoD1: a nuclear phosphoprotein requiring a Myc homology region to convert fibroblasts to myoblasts. Science. 1988 Oct 21;242(4877):405-11. PMID:3175662

1mdy, resolution 2.80Å

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