6czs

Crystal structure of human pro-cathepsin H C26S mutant

spinqualitylabelsall models 6czs, resolution 1.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6czs 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 1.66Å Ligands: BMA, CL, GLC, MAN, NAG, PRD_900006, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease CATH_HUMAN Narcolepsy-cataplexy. Function CATH_HUMAN Important for the overall degradation of proteins in lysosomes. Publication Abstract from PubMed Cathepsin H is a member of the papain superfamily of lysosomal cysteine proteases. It is the only known aminopeptidase in the family and is reported to be involved in cancer and other major diseases. Like many other proteases, it is synthesized as an inactive proenzyme. Although the crystal structure of mature porcine cathepsin H revealed the binding of the mini-chain and provided structural basis for the aminopeptidase activity, detailed structural and functional information on the inhibition and activation of procathepsin H has been elusive. Here we present the crystal structures of human procathepsin H at 2.00 A and 1.66 A resolution. These structures allow us to explore in detail the molecular basis for the inhibition of the mature domain by the prodomain. Comparison with cathepsin H structure reveals how mini-chain reorients upon activation. We further demonstrate that procathepsin H is not auto-activated but can be trans-activated by cathepsin L. Crystal structures of human procathepsin H.,Hao Y, Purtha W, Cortesio C, Rui H, Gu Y, Chen H, Sickmier EA, Manzanillo P, Huang X PLoS One. 2018 Jul 25;13(7):e0200374. doi: 10.1371/journal.pone.0200374., eCollection 2018. PMID:30044821 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cathepsin 3D structures

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