1p47
From Proteopedia
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Crystal Structure of tandem Zif268 molecules complexed to DNA
Overview
Zinc-finger proteins offer a versatile and effective framework for the, recognition of DNA binding sites. By connecting multiple fingers together, with canonical TGEKP linkers, a protein may be designed to recognize, almost any desired target DNA sequence. However, proteins containing more, than three zinc-fingers do not bind as tightly as one might predict, and, it appears that some type of strain is introduced when a six-finger, protein is constructed with canonical linkers. In an attempt to understand, the sources of this strain, we have solved the 2.2A resolution X-ray, crystallographic structure of a complex that has two copies of the, three-finger Zif268 protein bound to adjacent sites on one duplex DNA., Conceptually, this is equivalent to a six-finger protein in which the, central linker has been removed and the complex has been allowed to, "relax" to its most stable conformation. As in other Zif268-DNA complexes, the DNA is approximately linear and is slightly underwound. Surprisingly, the structure of the complex is similar (within 0.5A) to an arrangement, that would allow a canonical linker at the center of the complex, and it, seems possible that entropic effects (involving the librational degrees of, freedom in the complex) could be important in determining optimal linker, length.
About this Structure
1P47 is a Single protein structure of sequence from Mus musculus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Constraints for zinc finger linker design as inferred from X-ray crystal structure of tandem Zif268-DNA complexes., Peisach E, Pabo CO, J Mol Biol. 2003 Jun 27;330(1):1-7. PMID:12818197
Page seeded by OCA on Tue Nov 20 23:27:45 2007
