1a1f
From Proteopedia
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| - | [[Image:1a1f.gif|left|200px]] | + | [[Image:1a1f.gif|left|200px]] |
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| - | '''DSNR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GACC SITE)''' | + | {{Structure |
| + | |PDB= 1a1f |SIZE=350|CAPTION= <scene name='initialview01'>1a1f</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''DSNR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GACC SITE)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A1F is a [ | + | 1A1F 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=1A1F 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]] | [[Category: zinc finger]] | ||
| - | ''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 09:51:31 2008'' |
Revision as of 07:51, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
DSNR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GACC 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
1A1F 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
Page seeded by OCA on Thu Mar 20 09:51:31 2008
