5i4h

Caught in the Act: The Crystal Structure of cleaved Cathepsin L bound to the active site of Cathepsin L

spinqualitylabelsall models 5i4h, resolution 1.42Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5i4h is a 2 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 1.42Å Ligands: GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CATL1_HUMAN Important for the overall degradation of proteins in lysosomes. Publication Abstract from PubMed Cathepsin L is a ubiquitously expressed papain-like cysteine protease involved in the endosomal degradation of proteins and has numerous roles in physiological and pathological processes, such as arthritis, osteoporosis, and cancer. Insight into the specificity of cathepsin L is important for elucidating its physiological roles and drug discovery. To study interactions with synthetic ligands, we prepared a presumably inactive mutant and crystallized it. Unexpectedly, the crystal structure determined at 1.4 A revealed that the cathepsin L molecule is cleaved, with the cleaved region trapped in the active site cleft of the neighboring molecule. Hence, the catalytic mutant demonstrated low levels of catalytic activity. Caught in the act: the crystal structure of cleaved cathepsin L bound to the active site of Cathepsin L.,Sosnowski P, Turk D FEBS Lett. 2016 Apr;590(8):1253-61. doi: 10.1002/1873-3468.12140. Epub 2016 Mar, 30. PMID:26992470 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cathepsin 3D structures

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