5onp: Difference between revisions
Jump to navigation
Jump to search
m Protected "5onp" [edit=sysop:move=sysop] |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==Alzheimer's Amyloid-Beta Peptide Fragment 1-40 in Complex with Cd-substituted Thermolysin== | ||
<StructureSection load='5onp' size='340' side='right'caption='[[5onp]], [[Resolution|resolution]] 1.34Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5onp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ONP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ONP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.34Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5onp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5onp OCA], [https://pdbe.org/5onp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5onp RCSB], [https://www.ebi.ac.uk/pdbsum/5onp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5onp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/THER_GEOSE THER_GEOSE] Extracellular zinc metalloprotease.<ref>PMID:3149972</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:30403288</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5onp" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Thermolysin 3D structures|Thermolysin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Geobacillus stearothermophilus]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Gales L]] | |||
[[Category: Leite JP]] | |||
Latest revision as of 19:55, 13 December 2023
Alzheimer's Amyloid-Beta Peptide Fragment 1-40 in Complex with Cd-substituted ThermolysinAlzheimer's Amyloid-Beta Peptide Fragment 1-40 in Complex with Cd-substituted Thermolysin
Structural highlights
FunctionTHER_GEOSE Extracellular zinc metalloprotease.[1] Publication Abstract from PubMedThe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||