1ozj: Difference between revisions
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[[Image:1ozj.gif|left|200px]] | [[Image:1ozj.gif|left|200px]] | ||
'''Crystal structure of Smad3-MH1 bound to DNA at 2.4 A resolution''' | {{Structure | ||
|PDB= 1ozj |SIZE=350|CAPTION= <scene name='initialview01'>1ozj</scene>, resolution 2.4Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= | |||
|GENE= MADH3 OR SMAD3 OR MAD3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Crystal structure of Smad3-MH1 bound to DNA at 2.4 A resolution''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1OZJ is a [ | 1OZJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OZJ OCA]. | ||
==Reference== | ==Reference== | ||
Features of a Smad3 MH1-DNA complex. Roles of water and zinc in DNA binding., Chai J, Wu JW, Yan N, Massague J, Pavletich NP, Shi Y, J Biol Chem. 2003 May 30;278(22):20327-31. Epub 2003 Apr 9. PMID:[http:// | Features of a Smad3 MH1-DNA complex. Roles of water and zinc in DNA binding., Chai J, Wu JW, Yan N, Massague J, Pavletich NP, Shi Y, J Biol Chem. 2003 May 30;278(22):20327-31. Epub 2003 Apr 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12686552 12686552] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc-binding module]] | [[Category: zinc-binding module]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:17:46 2008'' | ||
Revision as of 14:17, 20 March 2008
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| , resolution 2.4Å | |||||||
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| Ligands: | |||||||
| Gene: | MADH3 OR SMAD3 OR MAD3 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Smad3-MH1 bound to DNA at 2.4 A resolution
OverviewOverview
The Smad family of proteins mediates transforming growth factor-beta signaling from cell membrane to the nucleus. In the nucleus, Smads serve as transcription factors by directly binding to specific DNA sequences and regulating the expression of ligand-response genes. A previous structural analysis, at 2.8-A resolution, revealed a novel DNA-binding mode for the Smad MH1 domain but did not allow accurate assignment of the fines features of protein-DNA interactions. The crystal structure of a Smad3 MH1 domain bound to a palindromic DNA sequence, determined at 2.4-A resolution, reveals a surprisingly important role for water molecules. The asymmetric placement of the DNA-binding motif (a conserved 11-residue beta-hairpin) in the major groove of DNA is buttressed by seven well ordered water molecules. These water molecules make specific hydrogen bonds to the DNA bases, the DNA phosphate backbones, and several critical Smad3 residues. In addition, the MH1 domain is found to contain a bound zinc atom using four invariant residues among Smad proteins, three cysteines and one histidine. Removal of the zinc atom results in compromised DNA binding activity. These results define the Smad MH1 domain as a zinc-coordinating module that exhibits unique DNA binding properties.
About this StructureAbout this Structure
1OZJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Features of a Smad3 MH1-DNA complex. Roles of water and zinc in DNA binding., Chai J, Wu JW, Yan N, Massague J, Pavletich NP, Shi Y, J Biol Chem. 2003 May 30;278(22):20327-31. Epub 2003 Apr 9. PMID:12686552
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