5sy1 | pdb_00005sy1

Structure of the STRA6 receptor for retinol uptake in complex with calmodulin

spinqualitylabelsall models 5sy1, resolution 3.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5sy1 is a 4 chain structure with sequence from [1] and Spodoptera frugiperda. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CLR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Vitamin A homeostasis is critical to normal cellular function. Retinol-binding protein (RBP) is the sole specific carrier in the bloodstream for hydrophobic retinol, the main form in which vitamin A is transported. The integral membrane receptor STRA6 mediates cellular uptake of vitamin A by recognizing RBP-retinol to trigger release and internalization of retinol. We present the structure of zebrafish STRA6 determined to 3.9-angstrom resolution by single-particle cryo-electron microscopy. STRA6 has one intramembrane and nine transmembrane helices in an intricate dimeric assembly. Unexpectedly, calmodulin is bound tightly to STRA6 in a noncanonical arrangement. Residues involved with RBP binding map to an archlike structure that covers a deep lipophilic cleft. This cleft is open to the membrane, suggesting a possible mode for internalization of retinol through direct diffusion into the lipid bilayer. Structure of the STRA6 receptor for retinol uptake.,Chen Y, Clarke OB, Kim J, Stowe S, Kim YK, Assur Z, Cavalier M, Godoy-Ruiz R, von Alpen DC, Manzini C, Blaner WS, Frank J, Quadro L, Weber DJ, Shapiro L, Hendrickson WA, Mancia F Science. 2016 Aug 26;353(6302). pii: aad8266. doi: 10.1126/science.aad8266. PMID:27563101 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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