1a1h
From Proteopedia
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|PDB= 1a1h |SIZE=350|CAPTION= <scene name='initialview01'>1a1h</scene>, resolution 1.600Å | |PDB= 1a1h |SIZE=350|CAPTION= <scene name='initialview01'>1a1h</scene>, resolution 1.600Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a1h OCA], [http://www.ebi.ac.uk/pdbsum/1a1h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a1h RCSB]</span> | ||
}} | }} | ||
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[[Category: Elrod-Erickson, M.]] | [[Category: Elrod-Erickson, M.]] | ||
[[Category: Pabo, C O.]] | [[Category: Pabo, C O.]] | ||
| - | [[Category: ZN]] | ||
[[Category: complex (zinc finger/dna)]] | [[Category: complex (zinc finger/dna)]] | ||
[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:31:07 2008'' |
Revision as of 15:31, 30 March 2008
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| , resolution 1.600Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
QGSR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCAC SITE)
Overview
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 Structure
1A1H is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
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:9562555
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