2adr: Difference between revisions
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[[Image:2adr.jpg|left|200px]]< | [[Image:2adr.jpg|left|200px]] | ||
'''ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES''' | {{Structure | ||
|PDB= 2adr |SIZE=350|CAPTION= <scene name='initialview01'>2adr</scene> | |||
|SITE= <scene name='pdbsite=ZNC:Zn+Finger+2'>ZNC</scene> | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2ADR is a [ | 2ADR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ADR OCA]. | ||
==Reference== | ==Reference== | ||
A folding transition and novel zinc finger accessory domain in the transcription factor ADR1., Bowers PM, Schaufler LE, Klevit RE, Nat Struct Biol. 1999 May;6(5):478-85. PMID:[http:// | A folding transition and novel zinc finger accessory domain in the transcription factor ADR1., Bowers PM, Schaufler LE, Klevit RE, Nat Struct Biol. 1999 May;6(5):478-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10331877 10331877] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
''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 15:48:24 2008'' | ||
Revision as of 13:48, 20 March 2008
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| Sites: | ZNC | ||||||||||||
| Ligands: | ZN | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES
Overview
The region responsible for sequence-specific DNA binding by the transcription factor ADR1 contains two Cys2-His2 zinc fingers and an additional N-terminal proximal accessory region (PAR). The N-terminal (non-finger) PAR is unstructured in the absence of DNA and undergoes a folding transition on binding the DNA transcription target site. We have used a set of HN-HN NOEs derived from a perdeuterated protein-DNA complex to describe the fold of ADR1 bound to the UAS1 binding site. The PAR forms a compact domain consisting of three antiparallel strands that contact A-T base pairs in the major groove. The three-strand domain is a novel fold among all known DNA-binding proteins. The PAR shares sequence homology with the N-terminal regions of other zinc finger proteins, suggesting that it represents a new DNA-binding module that extends the binding repertoire of zinc finger proteins.
About this Structure
2ADR is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
A folding transition and novel zinc finger accessory domain in the transcription factor ADR1., Bowers PM, Schaufler LE, Klevit RE, Nat Struct Biol. 1999 May;6(5):478-85. PMID:10331877
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