CRALBP is important in the processing of retinal derivatives in the eye. Retinal serves as the photo-sensitive chromophore in the vision system where it is bound to the photopigment proteins. Its photo-induced conformation change while bound to rhodopsin and the cone opsins is the first molecular step in vision.
After a photon is absorbed by a photopigment protein, the retinal group needs to be regenerated in the active conformation. This involves transfer of the retinal out of the photoreceptor rod and cone cells into surrounding epithelial cells. There the retinal is processed in a series of chemical steps to regenerate the native conformation. Then the molecule is transferred back to the rods and cones. Throughout this process, the retinal is carried by special binding proteins. CRALBP is one of these carrier proteins.
Our work on CRALBP has focused on the determination of its molecular structure. We have tried to obtain crystals of the protein for X-ray crystallographic studies, but the protein is not amenable to crystallization. We are also working on using homology modeling methods to generate a structural model of the protein based on related proteins with similar amino acid sequences.
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