2adr: Difference between revisions

Revision as of 17:26, 21 February 2008

ADR1 DNA-BINDING DOMAIN FROM SACCHAROMYCES CEREVISIAE, NMR, 25 STRUCTURES

OverviewOverview

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 StructureAbout this Structure

2ADR is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 16:26:23 2008

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OCA

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 ==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.
+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==
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 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Bowers, P.M.]]
+[[Category: Bowers, P M.]]
-[[Category: Kleivt, R.E.]]
+[[Category: Kleivt, R E.]]
 [[Category: ZN]]
 [[Category: adr1]]
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 [[Category: zinc finger]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:22:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:26:23 2008''