6zfw
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X-ray structure of the soluble N-terminal domain of T. cruzi PEX-14
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Structural highlights
FunctionQ4D1H5_TRYCC Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.[RuleBase:RU367032] Publication Abstract from PubMedWe develop a residual deep learning model, hotWater (https://pypi.org/project/hotWater/), to identify key water interaction sites on proteins for binding models and drug discovery. This is tested on new crystal structures, as well as cryo-EM and NMR structures from the PDB and in crystallographic refinement with promising results. Deep learning model predicts water interaction sites on the surface of proteins using limited-resolution data.,Zaucha J, Softley CA, Sattler M, Frishman D, Popowicz GM Chem Commun (Camb). 2020 Nov 25. doi: 10.1039/d0cc04383d. PMID:33237041[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 13:48, 24 January 2024.