1mhd: Difference between revisions
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|PDB= 1mhd |SIZE=350|CAPTION= <scene name='initialview01'>1mhd</scene>, resolution 2.8Å | |PDB= 1mhd |SIZE=350|CAPTION= <scene name='initialview01'>1mhd</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= SMAD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= SMAD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhd OCA], [http://www.ebi.ac.uk/pdbsum/1mhd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mhd RCSB]</span> | |||
}} | }} | ||
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[[Category: smad3 mh1]] | [[Category: smad3 mh1]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:16:04 2008'' | ||
Revision as of 19:16, 30 March 2008
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| 1mhd, resolution 2.8Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | DA, DC, DG, DT | ||||||||||||
| Gene: | SMAD (Homo sapiens) | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF A SMAD MH1 DOMAIN BOUND TO DNA
Overview
The Smad family of proteins, which are frequently targeted by tumorigenic mutations in cancer, mediate TGF-beta signaling from cell membrane to nucleus. The crystal structure of a Smad3 MH1 domain bound to an optimal DNA sequence determined at 2.8 A resolution reveals a novel DNA-binding motif. In the crystals, base-specific DNA recognition is provided exclusively by a conserved 11-residue beta hairpin that is embedded in the major groove of DNA. A surface loop region, to which tumorigenic mutations map, has been identified as a functional surface important for Smad activity. This structure establishes a framework for understanding how Smad proteins may act in concert with other transcription factors in the regulation of TGF-beta-responsive genes.
About this Structure
1MHD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of a Smad MH1 domain bound to DNA: insights on DNA binding in TGF-beta signaling., Shi Y, Wang YF, Jayaraman L, Yang H, Massague J, Pavletich NP, Cell. 1998 Sep 4;94(5):585-94. PMID:9741623
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