6x48

Sortilin-Progranulin Interaction With Compound 17

spinqualitylabelsall models 6x48, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: BMA, GOL, MAN, NAG, UNL, UP4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed High-throughput screening methods have been used to identify two novel series of inhibitors that disrupt progranulin binding to sortilin. Exploration of structure-activity relationships (SAR) resulted in compounds with sufficient potency and physicochemical properties to enable co-crystallization with sortilin. These co-crystal structures supported observed SAR trends and provided guidance for additional avenues for designing compounds with additional interactions within the binding site. Identification of potent inhibitors of the sortilin-progranulin interaction.,Stachel SJ, Ginnetti AT, Johnson SA, Cramer P, Wang Y, Bukhtiyarova M, Krosky D, Stump C, Hurzy DM, Schlegel KA, Cooke AJ, Allen S, O'Donnell G, Ziebell M, Parthasarathy G, Getty KL, Ho T, Ou Y, Jovanovska A, Carroll SS, Pausch M, Lumb K, Mosser SD, Voleti B, Klein DJ, Soisson SM, Zerbinatti C, Coleman PJ Bioorg Med Chem Lett. 2020 Sep 1;30(17):127403. doi: 10.1016/j.bmcl.2020.127403. , Epub 2020 Jul 15. PMID:32738972 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Neurotensin receptor

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