1mdy

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[[Image:1mdy.gif|left|200px]]
[[Image:1mdy.gif|left|200px]]
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{{Structure
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|PDB= 1mdy |SIZE=350|CAPTION= <scene name='initialview01'>1mdy</scene>, resolution 2.800&Aring;
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The line below this paragraph, containing "STRUCTURE_1mdy", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>
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|GENE=
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{{STRUCTURE_1mdy| PDB=1mdy | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mdy OCA], [http://www.ebi.ac.uk/pdbsum/1mdy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mdy RCSB]</span>
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'''CRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION'''
'''CRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION'''
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[[Category: Rould, M A.]]
[[Category: Rould, M A.]]
[[Category: Weintraub, H.]]
[[Category: Weintraub, H.]]
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[[Category: protein-dna complex]]
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[[Category: Protein-dna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:55:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:14:55 2008''
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Revision as of 21:55, 2 May 2008

Template:STRUCTURE 1mdy

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


Overview

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.

About this Structure

1MDY is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

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:8181063 Page seeded by OCA on Sat May 3 00:55:38 2008

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