1mm3
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Solution structure of the 2nd PHD domain from Mi2b with C-terminal loop replaced by corresponding loop from WSTF
OverviewOverview
The design of proteins with tailored functions remains a relatively, elusive goal. Small size, a well-defined structure, and the ability to, maintain structural integrity despite multiple mutations are all desirable, properties for such designer proteins. Many zinc binding domains fit this, description. We determined the structure of a PHD finger from the, transcriptional cofactor Mi2beta and investigated the suitability of this, domain as a scaffold for presenting selected binding functions. The two, flexible loops in the structure were mutated extensively by either, substitution or expansion, without affecting the overall fold of the, domain. A binding site for the corepressor CtBP2 was also grafted onto the, domain, creating a new PHD domain that can specifically bind CtBP2 both in, vitro and in the context of a eukaryotic cell nucleus. These results, represent a step toward designing new regulatory proteins for modulating, aberrant gene expression in vivo.
About this StructureAbout this Structure
1MM3 is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Engineering a protein scaffold from a PHD finger., Kwan AH, Gell DA, Verger A, Crossley M, Matthews JM, Mackay JP, Structure. 2003 Jul;11(7):803-13. PMID:12842043
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