2lkt: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(7 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 2lkt is ON HOLD  until Paper Publication
==Solution structure of N-terminal domain of human TIG3 in 2 M UREA==
 
<StructureSection load='2lkt' size='340' side='right'caption='[[2lkt]]' scene=''>
Authors: Wang, L., Yu, W., Xia, B.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2lkt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LKT FirstGlance]. <br>
Description: Solution structure of N-terminal domain of human TIG3
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkt OCA], [https://pdbe.org/2lkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lkt RCSB], [https://www.ebi.ac.uk/pdbsum/2lkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lkt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PLAT4_HUMAN PLAT4_HUMAN] Exhibits both phospholipase A1/2 and acyltransferase activities (PubMed:19615464, PubMed:22605381, PubMed:22825852, PubMed:26503625). Shows phospholipase A1 (PLA1) and A2 (PLA2), catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (PubMed:19615464, PubMed:22605381, PubMed:22825852). For most substrates, PLA1 activity is much higher than PLA2 activity (PubMed:19615464). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (PubMed:19615464). Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs) (PubMed:19615464, PubMed:22605381, PubMed:22825852). Promotes keratinocyte differentiation via activation of TGM1 (PubMed:17762858).<ref>PMID:17762858</ref> <ref>PMID:19615464</ref> <ref>PMID:22605381</ref> <ref>PMID:22825852</ref> <ref>PMID:26503625</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Wang L]]
[[Category: Xia B]]
[[Category: Yu W]]

Latest revision as of 06:56, 1 May 2024

Solution structure of N-terminal domain of human TIG3 in 2 M UREA

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA