6e4l

The structure of the N-terminal domain of human clathrin heavy chain 1 (nTD) in complex with ES9

spinqualitylabelsall models 6e4l, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6e4l is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: ACT, DMS, EDO, GOL, HRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease CLH1_HUMAN Translocation renal cell carcinoma;Inflammatory myofibroblastic tumor. Function CLH1_HUMAN Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. Publication Abstract from PubMed Clathrin-mediated endocytosis (CME) is a highly conserved and essential cellular process in eukaryotic cells, but its dynamic and vital nature makes it challenging to study using classical genetics tools. In contrast, although small molecules can acutely and reversibly perturb CME, the few chemical CME inhibitors that have been applied to plants are either ineffective or show undesirable side effects. Here, we identify the previously described endosidin9 (ES9) as an inhibitor of clathrin heavy chain (CHC) function in both Arabidopsis and human cells through affinity-based target isolation, in vitro binding studies and X-ray crystallography. Moreover, we present a chemically improved ES9 analog, ES9-17, which lacks the undesirable side effects of ES9 while retaining the ability to target CHC. ES9 and ES9-17 have expanded the chemical toolbox used to probe CHC function, and present chemical scaffolds for further design of more specific and potent CHC inhibitors across different systems. Disruption of endocytosis through chemical inhibition of clathrin heavy chain function.,Dejonghe W, Sharma I, Denoo B, De Munck S, Lu Q, Mishev K, Bulut H, Mylle E, De Rycke R, Vasileva M, Savatin DV, Nerinckx W, Staes A, Drozdzecki A, Audenaert D, Yperman K, Madder A, Friml J, Van Damme D, Gevaert K, Haucke V, Savvides SN, Winne J, Russinova E Nat Chem Biol. 2019 Apr 22. pii: 10.1038/s41589-019-0262-1. doi:, 10.1038/s41589-019-0262-1. PMID:31011214 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Clathrin 3D structures

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