Difference between revisions of "Part:BBa K364204"

Revision as of 19:40, 21 September 2011

DBD designed for RARE in CD38

Zinc finger polymer design to bind to RARE in cyclic ADP ribose hidrolase (CD38).

Zinc fingers are small protein structural motifs binding one or more zinc ions to help stabilize their folds. Zinc finger proteins often bind to DNA and RNA because their shape allows close interaction of the domain with the nucleotides of DNA and RNA, and they can also bind to proteins and small molecules. Their nucleotide binding properties allow them to function in regulating gene expression and in virus assembly.

Zinc fingers coordinate zinc ions with a combination of cysteine and histidine residues. They can be classified by the type and order of these zinc coordinating residues (e.g., Cys2His2, Cys4, and Cys6). A more systematic method classifies them into different "fold groups" based on the overall shape of the protein backbone in the folded domain. The most common "fold groups" of zinc fingers are the Cys2His2-like (the "classic zinc finger"), treble clef, and zinc ribbon. The DNA binding domain of nuclear hormone receptors is a highly conserved domain containing two zinc fingers that binds to specific sequences of DNA called hormone response elements (HRE).

Zinc finger protein competes with endogenous RAR without RAR agonist ligand. The numbers show the ratio between the ZN-FINGERS and the buffer plasmids: 1.ZN-FINGERS:buffer plasmids-1:8; 2.ZN-FINGERS:buffer plasmids-1:2; 3.Only ZN-FINGERS.

Zinc finger protein competes with endogenous RAR in the presence of RAR agonist ligand. The numbers show the ratio between the ZN-FINGERS and the buffer plasmids: 1.ZN-FINGERS:buffer plasmids-1:8; 2.ZN-FINGERS:buffer plasmids-1:2; 3.Only ZN-FINGERS.

Sequence and Features