1xgg

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

THEORETICAL MODEL OF THE CELLULAR RETINALDEHYDE BINDING PROTEIN IN ITS CLOSED CONFORMATIONTHEORETICAL MODEL OF THE CELLULAR RETINALDEHYDE BINDING PROTEIN IN ITS CLOSED CONFORMATION

Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed Cellular retinaldehyde-binding protein (CRALBP) is an essential protein in the human visual cycle without a known three-dimensional structure. Previous studies associate retinal pathologies to specific mutations in the CRALBP protein. Here we use homology modeling and molecular dynamics methods to investigate the structural mechanisms by which CRALBP functions in the visual cycle. We have constructed two conformations of CRALBP representing two states in the process of ligand association and dissociation. Notably, our homology models map the pathology-associated mutations either directly in or adjacent to the putative ligand-binding cavity. Furthermore, six novel residues have been identified to be crucial for the hinge movement of the lipid-exchange loop in CRALBP. We conclude that the binding and release of retinoid involve large conformational changes in the lipid-exchange loop at the entrance of the ligand-binding cavity. Structural insights into the cellular retinaldehyde-binding protein (CRALBP).,Liu T, Jenwitheesuk E, Teller DC, Samudrala R Proteins. 2005 Nov 1;61(2):412-22. PMID:16121400 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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