1sp1
From Proteopedia
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==Overview== | ==Overview== | ||
The carboxyl terminus of transcription factor Sp1 contains three, contiguous Cys2-His2 zinc finger domains with the consensus sequence, Cys-X2-4-Cys-X12-His-X3-His. We have used standard homonuclear, two-dimensional NMR techniques to solve the solution structures of, synthetic peptides corresponding to the last two zinc finger domains, (Sp1f2 and Sp1f3, respectively) of Sp1. Our studies indicate a classical, Cys2-His2 type fold for both the domains differing from each other, primarily in the conformation of Cys-X2-Cys (beta-type I turn) and, Cys-X4-Cys (beta-type II turn) elements. There are, however, no, significant differences in the metal binding properties between the, Cys-X4-Cys (Sp1f2) and Cys-X2-Cys (Sp1f3) subclasses of zinc fingers. The, free solution structures of Sp1f2 and Sp1f3 are very similar to those of, the analogous fingers of Zif268 bound to DNA. There is NMR spectral, evidence suggesting that the Arg-Asp buttressing interaction observed in, the Zif-268.DNA complex is also preserved in unbound Sp1f2 and Sp1f3., Modeling Sp1-DNA complex by overlaying the Sp1f2 and Sp1f3 structures on, Zif268 fingers 1 and 2, respectively, predicts the role of key amino acid, residues, the interference/protection data, and supports the model of, Sp1-DNA interaction proposed earlier. | The carboxyl terminus of transcription factor Sp1 contains three, contiguous Cys2-His2 zinc finger domains with the consensus sequence, Cys-X2-4-Cys-X12-His-X3-His. We have used standard homonuclear, two-dimensional NMR techniques to solve the solution structures of, synthetic peptides corresponding to the last two zinc finger domains, (Sp1f2 and Sp1f3, respectively) of Sp1. Our studies indicate a classical, Cys2-His2 type fold for both the domains differing from each other, primarily in the conformation of Cys-X2-Cys (beta-type I turn) and, Cys-X4-Cys (beta-type II turn) elements. There are, however, no, significant differences in the metal binding properties between the, Cys-X4-Cys (Sp1f2) and Cys-X2-Cys (Sp1f3) subclasses of zinc fingers. The, free solution structures of Sp1f2 and Sp1f3 are very similar to those of, the analogous fingers of Zif268 bound to DNA. There is NMR spectral, evidence suggesting that the Arg-Asp buttressing interaction observed in, the Zif-268.DNA complex is also preserved in unbound Sp1f2 and Sp1f3., Modeling Sp1-DNA complex by overlaying the Sp1f2 and Sp1f3 structures on, Zif268 fingers 1 and 2, respectively, predicts the role of key amino acid, residues, the interference/protection data, and supports the model of, Sp1-DNA interaction proposed earlier. | ||
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| + | ==Disease== | ||
| + | Known diseases associated with this structure: Hepatic venoocclusive disease with immunodeficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604457 604457]], Mycobacterium tuberculosis, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604457 604457]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:16:33 2007'' |
Revision as of 17:10, 12 November 2007
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NMR STRUCTURE OF A ZINC FINGER DOMAIN FROM TRANSCRIPTION FACTOR SP1F3, MINIMIZED AVERAGE STRUCTURE
Contents |
Overview
The carboxyl terminus of transcription factor Sp1 contains three, contiguous Cys2-His2 zinc finger domains with the consensus sequence, Cys-X2-4-Cys-X12-His-X3-His. We have used standard homonuclear, two-dimensional NMR techniques to solve the solution structures of, synthetic peptides corresponding to the last two zinc finger domains, (Sp1f2 and Sp1f3, respectively) of Sp1. Our studies indicate a classical, Cys2-His2 type fold for both the domains differing from each other, primarily in the conformation of Cys-X2-Cys (beta-type I turn) and, Cys-X4-Cys (beta-type II turn) elements. There are, however, no, significant differences in the metal binding properties between the, Cys-X4-Cys (Sp1f2) and Cys-X2-Cys (Sp1f3) subclasses of zinc fingers. The, free solution structures of Sp1f2 and Sp1f3 are very similar to those of, the analogous fingers of Zif268 bound to DNA. There is NMR spectral, evidence suggesting that the Arg-Asp buttressing interaction observed in, the Zif-268.DNA complex is also preserved in unbound Sp1f2 and Sp1f3., Modeling Sp1-DNA complex by overlaying the Sp1f2 and Sp1f3 structures on, Zif268 fingers 1 and 2, respectively, predicts the role of key amino acid, residues, the interference/protection data, and supports the model of, Sp1-DNA interaction proposed earlier.
Disease
Known diseases associated with this structure: Hepatic venoocclusive disease with immunodeficiency OMIM:[604457], Mycobacterium tuberculosis, susceptibility to OMIM:[604457]
About this Structure
1SP1 is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Structure known Active Site: S1. Full crystallographic information is available from OCA.
Reference
Structures of zinc finger domains from transcription factor Sp1. Insights into sequence-specific protein-DNA recognition., Narayan VA, Kriwacki RW, Caradonna JP, J Biol Chem. 1997 Mar 21;272(12):7801-9. PMID:9065444
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