1a1j: Difference between revisions
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[[Image:1a1j.gif|left|200px]] | [[Image:1a1j.gif|left|200px]] | ||
'''RADR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCGT SITE)''' | {{Structure | ||
|PDB= 1a1j |SIZE=350|CAPTION= <scene name='initialview01'>1a1j</scene>, resolution 2.000Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''RADR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCGT SITE)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1A1J is a [ | 1A1J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A1J OCA]. | ||
==Reference== | ==Reference== | ||
High-resolution structures of variant Zif268-DNA complexes: implications for understanding zinc finger-DNA recognition., Elrod-Erickson M, Benson TE, Pabo CO, Structure. 1998 Apr 15;6(4):451-64. PMID:[http:// | High-resolution structures of variant Zif268-DNA complexes: implications for understanding zinc finger-DNA recognition., Elrod-Erickson M, Benson TE, Pabo CO, Structure. 1998 Apr 15;6(4):451-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9562555 9562555] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc finger-dna complex]] | [[Category: zinc finger-dna complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:51:32 2008'' | ||
Revision as of 10:51, 20 March 2008
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RADR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCGT SITE)
OverviewOverview
BACKGROUND: Zinc fingers of the Cys2-His2 class comprise one of the largest families of eukaryotic DNA-binding motifs and recognize a diverse set of DNA sequences. These proteins have a relatively simple modular structure and key base contacts are typically made by a few residues from each finger. These features make the zinc finger motif an attractive system for designing novel DNA-binding proteins and for exploring fundamental principles of protein-DNA recognition. RESULTS: Here we report the X-ray crystal structures of zinc finger-DNA complexes involving three variants of Zif268, with multiple changes in the recognition helix of finger one. We describe the structure of each of these three-finger peptides bound to its corresponding target site. To help elucidate the differential basis for site-specific recognition, the structures of four other complexes containing various combinations of these peptides with alternative binding sites have also been determined. CONCLUSIONS: The protein-DNA contacts observed in these complexes reveal the basis for the specificity demonstrated by these Zif268 variants. Many, but not all, of the contacts can be rationalized in terms of a recognition code, but the predictive value of such a code is limited. The structures illustrate how modest changes in the docking arrangement accommodate the new sidechain-base and sidechain-phosphate interactions. Such adaptations help explain the versatility of naturally occurring zinc finger proteins and their utility in design.
About this StructureAbout this Structure
1A1J is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
High-resolution structures of variant Zif268-DNA complexes: implications for understanding zinc finger-DNA recognition., Elrod-Erickson M, Benson TE, Pabo CO, Structure. 1998 Apr 15;6(4):451-64. PMID:9562555
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