4han: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 1: Line 1:


==Crystal structure of Galectin 8 with NDP52 peptide==
==Crystal structure of Galectin 8 with NDP52 peptide==
<StructureSection load='4han' size='340' side='right' caption='[[4han]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
<StructureSection load='4han' size='340' side='right'caption='[[4han]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4han]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HAN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HAN FirstGlance]. <br>
<table><tr><td colspan='2'>[[4han]] is a 4 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=4HAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HAN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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]] 2.551&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CALCOCO2, NDP52 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4han FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4han OCA], [http://pdbe.org/4han PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4han RCSB], [http://www.ebi.ac.uk/pdbsum/4han PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4han ProSAT]</span></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=4han FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4han OCA], [https://pdbe.org/4han PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4han RCSB], [https://www.ebi.ac.uk/pdbsum/4han PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4han ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/LEG8_HUMAN LEG8_HUMAN]] Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.<ref>PMID:21288902</ref> [[http://www.uniprot.org/uniprot/CACO2_HUMAN CACO2_HUMAN]] May play a role in ruffle formation and actin cytoskeleton organization. Seems to negatively regulate constitutive secretion.<ref>PMID:17635994</ref> 
[https://www.uniprot.org/uniprot/LEG8_HUMAN LEG8_HUMAN] Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.<ref>PMID:21288902</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Infectious bacteria are cleared from mammalian cells by host autophagy in combination with other upstream cellular components, such as the autophagic receptor NDP52 and sugar receptor galectin-8. However, the detailed molecular basis of the interaction between these two receptors remains to be elucidated. Here, we report the biochemical characterization of both NDP52 and galectin-8 as well as the crystal structure of galectin-8 complexed with an NDP52 peptide. The unexpected observation of nicotinamide adenine dinucleotide located at the carbohydrate-binding site expands our knowledge of the sugar-binding specificity of galectin-8. The NDP52-galectin-8 complex structure explains the key determinants for recognition on both receptors and defines a special orientation of N- and C-terminal carbohydrate recognition domains of galectin-8. Dimeric NDP52 forms a ternary complex with two monomeric galectin-8 molecules as well as two LC3C molecules. These results lay the groundwork for understanding how host cells target bacterial pathogens for autophagy.


Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8.,Kim BW, Hong SB, Kim JH, Kwon do H, Song HK Nat Commun. 2013;4:1613. doi: 10.1038/ncomms2606. PMID:23511477<ref>PMID:23511477</ref>
==See Also==
 
*[[Galectin 3D structures|Galectin 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4han" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Hong, S B]]
[[Category: Large Structures]]
[[Category: Kim, B W]]
[[Category: Hong SB]]
[[Category: Kim, J H]]
[[Category: Kim B-W]]
[[Category: Kwon, D H]]
[[Category: Kim JH]]
[[Category: Song, H K]]
[[Category: Kwon DH]]
[[Category: Autophagy]]
[[Category: Song HK]]
[[Category: Autophagy adapter molecule]]
[[Category: Cytosol]]
[[Category: Innate immunity]]
[[Category: Nad binding]]
[[Category: Ndp52 peoptide binding]]
[[Category: Sugar binding protein]]

Latest revision as of 14:36, 1 March 2024

Crystal structure of Galectin 8 with NDP52 peptideCrystal structure of Galectin 8 with NDP52 peptide

Structural highlights

4han is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.551Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LEG8_HUMAN Lectin with a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans.[1]

See Also

References

  1. ↑ Ideo H, Matsuzaka T, Nonaka T, Seko A, Yamashita K. Galectin-8-N-domain recognition mechanism for sialylated and sulfated glycans. J Biol Chem. 2011 Apr 1;286(13):11346-55. Epub 2011 Feb 2. PMID:21288902 doi:10.1074/jbc.M110.195925

4han, resolution 2.55Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=4han&oldid=4073949"