1a1i: Difference between revisions
New page: left|200px<br /><applet load="1a1i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a1i, resolution 1.600Å" /> '''RADR (ZIF268 VARIAN... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1a1i.gif|left|200px]]<br /><applet load="1a1i" size=" | [[Image:1a1i.gif|left|200px]]<br /><applet load="1a1i" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1a1i, resolution 1.600Å" /> | caption="1a1i, resolution 1.600Å" /> | ||
'''RADR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCAC SITE)'''<br /> | '''RADR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCAC SITE)'''<br /> | ||
==Overview== | ==Overview== | ||
BACKGROUND: Zinc fingers of the Cys2-His2 class comprise one of the | 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== | ==About this Structure== | ||
1A1I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1A1I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A1I OCA]. | ||
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Benson, T | [[Category: Benson, T E.]] | ||
[[Category: Elrod-Erickson, M.]] | [[Category: Elrod-Erickson, M.]] | ||
[[Category: Pabo, C | [[Category: Pabo, C O.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
| Line 21: | Line 21: | ||
[[Category: zinc finger-dna complex]] | [[Category: zinc finger-dna complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:50 2008'' | ||
Revision as of 12:39, 21 February 2008
|
RADR (ZIF268 VARIANT) ZINC FINGER-DNA COMPLEX (GCAC 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
1A1I is a Single protein structure of sequence from Mus musculus with as ligand. 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
Page seeded by OCA on Thu Feb 21 11:39:50 2008