2zhm: Difference between revisions

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[[Image:2zhm.png|left|200px]]


{{STRUCTURE_2zhm|  PDB=2zhm  |  SCENE=  }}
==Crystal structure of human galectin-9 N-terminal CRD in complex with N-acetyllactosamine trimer (crystal 1)==
 
<StructureSection load='2zhm' size='340' side='right'caption='[[2zhm]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
===Crystal structure of human galectin-9 N-terminal CRD in complex with N-acetyllactosamine trimer (crystal 1)===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2zhm]] 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=2ZHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZHM FirstGlance]. <br>
{{ABSTRACT_PUBMED_18977853}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=RPN:(R)-1-PARA-NITRO-PHENYL-2-AZIDO-ETHANOL'>RPN</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zhm OCA], [https://pdbe.org/2zhm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zhm RCSB], [https://www.ebi.ac.uk/pdbsum/2zhm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zhm ProSAT]</span></td></tr>
[[2zhm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZHM OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/LEG9_HUMAN LEG9_HUMAN] Binds galactosides. Has high affinity for the Forssman pentasaccharide. May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. Inhibits cell proliferation. It is a ligand for HAVCR2/TIM3. Induces T-helper type 1 lymphocyte (Th1) death. Isoform Short acts as an eosinophil chemoattractant.<ref>PMID:16286920</ref> <ref>PMID:18005988</ref> <ref>PMID:18977853</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zh/2zhm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2zhm ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Galectin|Galectin]]
*[[Galectin 3D structures|Galectin 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:018977853</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Kato, R.]]
[[Category: Large Structures]]
[[Category: Murata, T.]]
[[Category: Kato R]]
[[Category: Nagae, M.]]
[[Category: Murata T]]
[[Category: Nakamura, T.]]
[[Category: Nagae M]]
[[Category: Nishi, N.]]
[[Category: Nakamura T]]
[[Category: Usui, T.]]
[[Category: Nishi N]]
[[Category: Wakatsuki, S.]]
[[Category: Usui T]]
[[Category: Beta sandwich]]
[[Category: Wakatsuki S]]
[[Category: Carbohydrate binding protein]]
[[Category: Galectin]]
[[Category: Sugar binding protein]]

Latest revision as of 16:57, 13 March 2024

Crystal structure of human galectin-9 N-terminal CRD in complex with N-acetyllactosamine trimer (crystal 1)Crystal structure of human galectin-9 N-terminal CRD in complex with N-acetyllactosamine trimer (crystal 1)

Structural highlights

2zhm 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 1.84Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LEG9_HUMAN Binds galactosides. Has high affinity for the Forssman pentasaccharide. May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. Inhibits cell proliferation. It is a ligand for HAVCR2/TIM3. Induces T-helper type 1 lymphocyte (Th1) death. Isoform Short acts as an eosinophil chemoattractant.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Zhu C, Anderson AC, Schubart A, Xiong H, Imitola J, Khoury SJ, Zheng XX, Strom TB, Kuchroo VK. The Tim-3 ligand galectin-9 negatively regulates T helper type 1 immunity. Nat Immunol. 2005 Dec;6(12):1245-52. Epub 2005 Nov 13. PMID:16286920 doi:http://dx.doi.org/10.1038/ni1271
  2. Nagae M, Nishi N, Nakamura-Tsuruta S, Hirabayashi J, Wakatsuki S, Kato R. Structural analysis of the human galectin-9 N-terminal carbohydrate recognition domain reveals unexpected properties that differ from the mouse orthologue. J Mol Biol. 2008 Jan 4;375(1):119-35. Epub 2007 Sep 26. PMID:18005988 doi:S0022-2836(07)01208-9
  3. Nagae M, Nishi N, Murata T, Usui T, Nakamura T, Wakatsuki S, Kato R. Structural analysis of the recognition mechanism of poly-N-acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain. Glycobiology. 2009 Feb;19(2):112-7. Epub 2008 Oct 31. PMID:18977853 doi:cwn121

2zhm, resolution 1.84Å

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OCA