7lf8: Difference between revisions
New page: '''Unreleased structure''' The entry 7lf8 is ON HOLD Authors: Ultsch, M., Kirchhofer, D. Description: Fab 6D12 bound to ApoL2 NTD Category: Unreleased Structures [[Category: Ultsch... |
No edit summary |
||
(3 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
The | ==Fab 6D12 bound to ApoL2 NTD== | ||
<StructureSection load='7lf8' size='340' side='right'caption='[[7lf8]], [[Resolution|resolution]] 2.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7lf8]] is a 3 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=7LF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LF8 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]] 2.15Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=7lf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lf8 OCA], [https://pdbe.org/7lf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lf8 RCSB], [https://www.ebi.ac.uk/pdbsum/7lf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lf8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/APOL2_HUMAN APOL2_HUMAN] May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Apolipoprotein L1 (ApoL1) is a circulating innate immunity protein protecting against trypanosome infection. However, two ApoL1 coding variants are associated with a highly increased risk of chronic kidney disease. Here we present X-ray and NMR structures of the N-terminal domain (NTD) of ApoL1 and of its closest relative ApoL2. In both proteins, four of the five NTD helices form a four-helix core structure which is different from the classical four-helix bundle and from the pore-forming domain of colicin A. The reactivity with a conformation-specific antibody and structural models predict that this four-helix motif is also present in the NTDs of ApoL3 and ApoL4, suggesting related functions within the small ApoL family. The long helix 5 of ApoL1 is conformationally flexible and contains the BH3-like region. This BH3-like alpha-helix resembles true BH3 domains only in sequence and structure but not in function, since it does not bind to the pro-survival members of the Bcl-2 family, suggesting a Bcl-2-independent role in cytotoxicity. These findings should expedite a more comprehensive structural and functional understanding of the ApoL immune protein family. | |||
Structures of the ApoL1 and ApoL2 N-terminal domains reveal a non-classical four-helix bundle motif.,Ultsch M, Holliday MJ, Gerhardy S, Moran P, Scales SJ, Gupta N, Oltrabella F, Chiu C, Fairbrother W, Eigenbrot C, Kirchhofer D Commun Biol. 2021 Jul 27;4(1):916. doi: 10.1038/s42003-021-02387-5. PMID:34316015<ref>PMID:34316015</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7lf8" style="background-color:#fffaf0;"></div> | ||
[[Category: Kirchhofer | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Kirchhofer D]] | |||
[[Category: Ultsch M]] |
Latest revision as of 18:46, 18 October 2023
Fab 6D12 bound to ApoL2 NTDFab 6D12 bound to ApoL2 NTD
Structural highlights
FunctionAPOL2_HUMAN May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles. Publication Abstract from PubMedApolipoprotein L1 (ApoL1) is a circulating innate immunity protein protecting against trypanosome infection. However, two ApoL1 coding variants are associated with a highly increased risk of chronic kidney disease. Here we present X-ray and NMR structures of the N-terminal domain (NTD) of ApoL1 and of its closest relative ApoL2. In both proteins, four of the five NTD helices form a four-helix core structure which is different from the classical four-helix bundle and from the pore-forming domain of colicin A. The reactivity with a conformation-specific antibody and structural models predict that this four-helix motif is also present in the NTDs of ApoL3 and ApoL4, suggesting related functions within the small ApoL family. The long helix 5 of ApoL1 is conformationally flexible and contains the BH3-like region. This BH3-like alpha-helix resembles true BH3 domains only in sequence and structure but not in function, since it does not bind to the pro-survival members of the Bcl-2 family, suggesting a Bcl-2-independent role in cytotoxicity. These findings should expedite a more comprehensive structural and functional understanding of the ApoL immune protein family. Structures of the ApoL1 and ApoL2 N-terminal domains reveal a non-classical four-helix bundle motif.,Ultsch M, Holliday MJ, Gerhardy S, Moran P, Scales SJ, Gupta N, Oltrabella F, Chiu C, Fairbrother W, Eigenbrot C, Kirchhofer D Commun Biol. 2021 Jul 27;4(1):916. doi: 10.1038/s42003-021-02387-5. PMID:34316015[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|