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Domain binding and function: C1 domains are approximately 50 aminoacids long, enriched in cysteines, and are involved in the recruitment of proteins to the membrane. Typically, C1 domains bind phorbol esters or diacylglycerol, which are necessary for membrane localization. With phorbol ester bound, the upper surface of the C1 domain forms a contiguous hydrophobic surface in the domain. This enables the region to be buried into the lipid bilayer stabilizing membrane insertion. The middle portion of the domain contains a number of basic residues that can interact with lipid headgroups in the membrane, while the lower half of the C1 domain contains two zinc-binding sites that are important to maintain the fold of the domain.
Structure Reference: Zhang, G. et al. (1995) Cell 81(6), 917À924.
Examples of Domain Proteins:
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| The C-terminal C1 domain of PKCdelta bound to phorbol ester (red). | |
