Proteopedia:Demo1

This page aims to quickly demonstrate some of the features available in Proteopedia pages:

• Text, images, as well as videos embedded in the page.
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• Molecular models that are 3D, animated and interactive.
• The green links, specific to Proteopedia. These serve to act on the displayed molecular model, changing it to a new molecular scene.

The zinc finger motif in proteinsThe zinc finger motif in proteins

The term "motif" when used in structural biology tends to refer to one of two cases: A particular amino-acid sequence that characterises a biochemical function. A set of secondary structure elements that defines a functional or structural role. There are a great number of protein sequence motifs identified, many of which have well defined structural or functional roles. One such example is the so-called zinc finger motif which is readily identified from the following consensus sequence pattern (where "X" represents any amino acid): Cys - X(2-4) - Cys - X(3) - Phe - X(5) - Leu - X(2) - His - X(3) - His Coordination of the zinc ion by 4 amino acid residues forces a particular folding of the protein backbone, giving rise to the nickname zinc finger: The example structure, displayed to the right, that serves to is that of Zif268 protein-DNA complex from Mus musculus. In this example (a C2H2 class zinc finger) the conserved and residues form ligands to a whose coordination is essential to stabilise the tertiary fold of the protein. The fold is important because it helps orientate the to bind to the . You can watch an explanation in this video:

spinqualitylabelsall models 3 zinc finger domains in the transcriptional regulator Zif268 (PDB entry 1aay) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

See alsoSee also

• More information about zinc fingers
• A list of proteins with zinc fingers

AcknowledgementAcknowledgement

This page was based on content from User:James D Watson/Structural Templates