8ath
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8ath]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ATH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ATH FirstGlance]. <br> | <table><tr><td colspan='2'>[[8ath]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ATH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ATH FirstGlance]. <br> | ||
| - | </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=8ath FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ath OCA], [https://pdbe.org/8ath PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ath RCSB], [https://www.ebi.ac.uk/pdbsum/8ath PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ath ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.366Å</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=8ath FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ath OCA], [https://pdbe.org/8ath PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ath RCSB], [https://www.ebi.ac.uk/pdbsum/8ath PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ath ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/LAMP1_HUMAN LAMP1_HUMAN] Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, | + | [https://www.uniprot.org/uniprot/LAMP1_HUMAN LAMP1_HUMAN] Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation, autophagy and cholesterol homeostasis (PubMed:37390818). Acts as an important regulator of lysosomal lumen pH regulation by acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for optimal hydrolase activity (PubMed:37390818). Also plays an important role in NK-cells cytotoxicity (PubMed:2022921, PubMed:23632890). Mechanistically, participates in cytotoxic granule movement to the cell surface and perforin trafficking to the lytic granule (PubMed:23632890). In addition, protects NK-cells from degranulation-associated damage induced by their own cytotoxic granule content (PubMed:23847195). Presents carbohydrate ligands to selectins (PubMed:7685349).<ref>PMID:2022921</ref> <ref>PMID:23632890</ref> <ref>PMID:23847195</ref> <ref>PMID:37390818</ref> <ref>PMID:7685349</ref> (Microbial infection) Acts as a receptor for Lassa virus glycoprotein (PubMed:24970085, PubMed:25972533, PubMed:27605678, PubMed:28448640). Promotes also fusion of the virus with host membrane in less acidic endosomes (PubMed:29295909).<ref>PMID:24970085</ref> <ref>PMID:25972533</ref> <ref>PMID:27605678</ref> <ref>PMID:28448640</ref> <ref>PMID:29295909</ref> (Microbial infection) Supports the FURIN-mediated cleavage of mumps virus fusion protein F by interacting with both FURIN and the unprocessed form but not the processed form of the viral protein F.<ref>PMID:32295904</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Current revision
CRYSTAL STRUCTURE OF LAMP1 IN COMPLEX WITH FAB-B.
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