1fv5: Difference between revisions
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'''SOLUTION STRUCTURE OF THE FIRST ZINC FINGER FROM THE DROSOPHILA U-SHAPED TRANSCRIPTION FACTOR'''<br /> | '''SOLUTION STRUCTURE OF THE FIRST ZINC FINGER FROM THE DROSOPHILA U-SHAPED TRANSCRIPTION FACTOR'''<br /> | ||
==Overview== | ==Overview== | ||
BACKGROUND: Zinc finger domains have traditionally been regarded as | BACKGROUND: Zinc finger domains have traditionally been regarded as sequence-specific DNA binding motifs. However, recent evidence indicates that many zinc fingers mediate specific protein-protein interactions. For instance, several zinc fingers from FOG family proteins have been shown to interact with the N-terminal zinc finger of GATA-1. RESULTS: We have used NMR spectroscopy to determine the first structures of two FOG family zinc fingers that are involved in protein-protein interactions: fingers 1 and 9 from U-shaped. These fingers resemble classical TFIIIA-like zinc fingers, with the exception of an unusual extended portion of the polypeptide backbone prior to the fourth zinc ligand. [15N,(1)H]-HSQC titrations have been used to define the GATA binding surface of USH-F1, and comparison with other FOG family proteins indicates that the recognition mechanism is conserved across species. The surface of FOG-type fingers that interacts with GATA-1 overlaps substantially with the surface through which classical fingers typically recognize DNA. This suggests that these fingers could not contact both GATA and DNA simultaneously. In addition, results from NMR, gel filtration, and sedimentation equilibrium experiments suggest that the interactions are of moderate affinity. CONCLUSIONS: Our results demonstrate unequivocally that zinc fingers comprising the classical betabetaalpha fold are capable of mediating specific contacts between proteins. The existence of this alternative function has implications for the prediction of protein function from sequence data and for the evolution of protein function. | ||
==About this Structure== | ==About this Structure== | ||
1FV5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1FV5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FV5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Crossley, M.]] | [[Category: Crossley, M.]] | ||
[[Category: Fox, A | [[Category: Fox, A H.]] | ||
[[Category: Kowalski, K.]] | [[Category: Kowalski, K.]] | ||
[[Category: Liew, C | [[Category: Liew, C K.]] | ||
[[Category: Mackay, J | [[Category: Mackay, J P.]] | ||
[[Category: Newton, A.]] | [[Category: Newton, A.]] | ||
[[Category: Sharpe, B | [[Category: Sharpe, B K.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: cchc]] | [[Category: cchc]] | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:56 2008'' | ||
Revision as of 13:42, 21 February 2008
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SOLUTION STRUCTURE OF THE FIRST ZINC FINGER FROM THE DROSOPHILA U-SHAPED TRANSCRIPTION FACTOR
OverviewOverview
BACKGROUND: Zinc finger domains have traditionally been regarded as sequence-specific DNA binding motifs. However, recent evidence indicates that many zinc fingers mediate specific protein-protein interactions. For instance, several zinc fingers from FOG family proteins have been shown to interact with the N-terminal zinc finger of GATA-1. RESULTS: We have used NMR spectroscopy to determine the first structures of two FOG family zinc fingers that are involved in protein-protein interactions: fingers 1 and 9 from U-shaped. These fingers resemble classical TFIIIA-like zinc fingers, with the exception of an unusual extended portion of the polypeptide backbone prior to the fourth zinc ligand. [15N,(1)H]-HSQC titrations have been used to define the GATA binding surface of USH-F1, and comparison with other FOG family proteins indicates that the recognition mechanism is conserved across species. The surface of FOG-type fingers that interacts with GATA-1 overlaps substantially with the surface through which classical fingers typically recognize DNA. This suggests that these fingers could not contact both GATA and DNA simultaneously. In addition, results from NMR, gel filtration, and sedimentation equilibrium experiments suggest that the interactions are of moderate affinity. CONCLUSIONS: Our results demonstrate unequivocally that zinc fingers comprising the classical betabetaalpha fold are capable of mediating specific contacts between proteins. The existence of this alternative function has implications for the prediction of protein function from sequence data and for the evolution of protein function.
About this StructureAbout this Structure
1FV5 is a Single protein structure of sequence from Drosophila melanogaster with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Solution structures of two CCHC zinc fingers from the FOG family protein U-shaped that mediate protein-protein interactions., Liew CK, Kowalski K, Fox AH, Newton A, Sharpe BK, Crossley M, Mackay JP, Structure. 2000 Nov 15;8(11):1157-66. PMID:11080638
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