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5ONQ

Alzheimer's Amyloid-Beta Peptide Fragment 29-40 in Complex with Cd-substituted Thermolysin

Summary for 5ONQ
Entry DOI10.2210/pdb5onq/pdb
Related5ONP
DescriptorThermolysin, Amyloid-beta A4 protein, CALCIUM ION, ... (6 entities in total)
Functional Keywordspeptidase, protein-peptide complex, amyloid-beta peptide, hydrolase
Biological sourceGeobacillus stearothermophilus (Bacillus stearothermophilus)
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Total number of polymer chains2
Total formula weight35357.70
Authors
Leite, J.P.,Gales, L. (deposition date: 2017-08-04, release date: 2018-08-29, Last modification date: 2024-01-17)
Primary citationLeite, J.P.,Gales, L.
Alzheimer's A beta1-40peptide degradation by thermolysin: evidence of inhibition by a C-terminal A beta product.
FEBS Lett., 593:128-137, 2019
Cited by
PubMed Abstract: The interaction of the amyloid-β peptide (Aβ) with thermolysin (TLN) was investigated by X-ray crystallography. Structural models of the complexes of TLN with several Aβ fragments show that, despite the numerous possible cleavage sites of the Aβ 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 Aβ clearance, suggests that NEP should be more efficient against Aβ 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 Aβ and its higher ability to degrade insoluble and/or oligomeric Aβ forms, producing only the Aβ intermediate.
PubMed: 30403288
DOI: 10.1002/1873-3468.13285
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.17 Å)
Structure validation

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