1fu9: Difference between revisions

Revision as of 03:57, 1 July 2008

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File:1fu9.png

Template:STRUCTURE 1fu9

SOLUTION STRUCTURE OF THE NINTH ZINC-FINGER DOMAIN OF THE U-SHAPED TRANSCRIPTION FACTORSOLUTION STRUCTURE OF THE NINTH ZINC-FINGER DOMAIN OF THE U-SHAPED TRANSCRIPTION FACTOR

Template:ABSTRACT PUBMED 11080638

About this StructureAbout this Structure

1FU9 is a Single protein structure of sequence from Drosophila melanogaster. Full experimental 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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OCA

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-'''SOLUTION STRUCTURE OF THE NINTH ZINC-FINGER DOMAIN OF THE U-SHAPED TRANSCRIPTION FACTOR'''
+===SOLUTION STRUCTURE OF THE NINTH ZINC-FINGER DOMAIN OF THE U-SHAPED TRANSCRIPTION FACTOR===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11080638}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11080638 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11080638}}
 ==About this Structure==
-FU9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FU9 OCA].
+FU9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FU9 OCA].
 ==Reference==
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 [[Category: Beta-hairpin + alpha-helix]]
 [[Category: Zinc-finger]]
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