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1zaa
From Proteopedia
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| , resolution 2.100Å | |||||||
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ZINC FINGER-DNA RECOGNITION: CRYSTAL STRUCTURE OF A ZIF268-DNA COMPLEX AT 2.1 ANGSTROMS
Overview
The zinc finger DNA-binding motif occurs in many proteins that regulate eukaryotic gene expression. The crystal structure of a complex containing the three zinc fingers from Zif268 (a mouse immediate early protein) and a consensus DNA-binding site has been determined at 2.1 angstroms resolution and refined to a crystallographic R factor of 18.2 percent. In this complex, the zinc fingers bind in the major groove of B-DNA and wrap part way around the double helix. Each finger has a similar relation to the DNA and makes its primary contacts in a three-base pair subsite. Residues from the amino-terminal portion of an alpha helix contact the bases, and most of the contracts are made with the guanine-rich strand of the DNA. This structure provides a framework for understanding how zinc fingers recognize DNA and suggests that this motif may provide a useful basis for the design of novel DNA-binding proteins.
About this Structure
1ZAA is a Single protein structure of sequence from Mus musculus. The following page contains interesting information on the relation of 1ZAA with [Zinc Fingers]. Full crystallographic information is available from OCA.
Reference
Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A., Pavletich NP, Pabo CO, Science. 1991 May 10;252(5007):809-17. PMID:2028256
Page seeded by OCA on Thu Mar 20 15:33:04 2008
