7dce | pdb_00007dce

Cryo-EM structure of human XKR8-basigin complex bound to Fab fragment

spinqualitylabelsall models 7dce, resolution 3.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7dce is a 4 chain structure with sequence from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.8Å Ligands: DLP, PCA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BASI_HUMAN Plays an important role in targeting the monocarboxylate transporters SLC16A1, SLC16A3 and SLC16A8 to the plasma membrane. Plays pivotal roles in spermatogenesis, embryo implantation, neural network formation and tumor progression. Stimulates adjacent fibroblasts to produce matrix metalloproteinases (MMPS). Seems to be a receptor for oligomannosidic glycans. In vitro, promotes outgrowth of astrocytic processes. Publication Abstract from PubMed Xkr8-Basigin is a plasma membrane phospholipid scramblase activated by kinases or caspases. We combined cryo-EM and X-ray crystallography to investigate its structure at an overall resolution of 3.8 A. Its membrane-spanning region carrying 22 charged amino acids adopts a cuboid-like structure stabilized by salt bridges between hydrophilic residues in transmembrane helices. Phosphatidylcholine binding was observed in a hydrophobic cleft on the surface exposed to the outer leaflet of the plasma membrane. Six charged residues placed from top to bottom inside the molecule were essential for scrambling phospholipids in inward and outward directions, apparently providing a pathway for their translocation. A tryptophan residue was present between the head group of phosphatidylcholine and the extracellular end of the path. Its mutation to alanine made the Xkr8-Basigin complex constitutively active, indicating that it plays a vital role in regulating its scramblase activity. The structure of Xkr8-Basigin provides insights into the molecular mechanisms underlying phospholipid scrambling. The tertiary structure of the human Xkr8-Basigin complex that scrambles phospholipids at plasma membranes.,Sakuragi T, Kanai R, Tsutsumi A, Narita H, Onishi E, Nishino K, Miyazaki T, Baba T, Kosako H, Nakagawa A, Kikkawa M, Toyoshima C, Nagata S Nat Struct Mol Biol. 2021 Oct;28(10):825-834. doi: 10.1038/s41594-021-00665-8. , Epub 2021 Oct 8. PMID:34625749 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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