5onp | pdb_00005onp

Alzheimer's Amyloid-Beta Peptide Fragment 1-40 in Complex with Cd-substituted Thermolysin

spinqualitylabelsall models 5onp, resolution 1.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5onp is a 2 chain structure with sequence from Geobacillus stearothermophilus and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.34Å Ligands: CA, CD, DMS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function THER_GEOSE Extracellular zinc metalloprotease. Publication Abstract from PubMed The interaction of the amyloid-beta peptide (Abeta) with thermolysin (TLN) was investigated by X-ray crystallography. Structural models of the complexes of TLN with several Abeta fragments show that, despite the numerous possible cleavage sites of the Abeta sequence, the C-terminal product of Ala30-Ile31 cleavage does not dissociate, thus inhibiting the enzyme. The high similarity between the TLN structural motif and neprilysin (NEP), the most extensively studied peptidase associated with Abeta clearance, suggests that NEP should be more efficient against Abeta polymorphs where Ala30-Ile31 is inaccessible, which is in agreement with studies in living mice that point to the limited role of NEP in degrading soluble Abeta and its higher ability to degrade insoluble and/or oligomeric Abeta forms, producing only the Abeta10-37 intermediate. Alzheimer's Abeta1-40 peptide degradation by thermolysin: evidence of inhibition by a C-terminal Abeta product.,Leite JP, Gales L FEBS Lett. 2019 Jan;593(1):128-137. doi: 10.1002/1873-3468.13285. Epub 2018 Nov, 23. PMID:30403288 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thermolysin 3D structures

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