2adr: Difference between revisions

Line 4:

==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==

Line 13:

[[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]]

Line 21:

[[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''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==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==
@@ Line 13: / Line 13: @@
 [[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]]
@@ Line 21: / Line 21: @@
 [[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''