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==Crystal structure of the MHC class II molecule I-Ag7 in complex with the peptide GAD221-235==
==Crystal structure of the MHC class II molecule I-Ag7 in complex with the peptide GAD221-235==
<StructureSection load='3cup' size='340' side='right' caption='[[3cup]], [[Resolution|resolution]] 3.09&Aring;' scene=''>
<StructureSection load='3cup' size='340' side='right'caption='[[3cup]], [[Resolution|resolution]] 3.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3cup]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CUP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CUP FirstGlance]. <br>
<table><tr><td colspan='2'>[[3cup]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CUP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 3.09&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H2-Aa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), H2-Ab1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=3cup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cup OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cup RCSB], [http://www.ebi.ac.uk/pdbsum/3cup PDBsum]</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=3cup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cup OCA], [https://pdbe.org/3cup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cup RCSB], [https://www.ebi.ac.uk/pdbsum/3cup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cup ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DCE2_RAT DCE2_RAT] Catalyzes the production of GABA.<ref>PMID:8999827</ref> [https://www.uniprot.org/uniprot/Q31135_MOUSE Q31135_MOUSE]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cu/3cup_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cu/3cup_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=3cup ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Major histocompatibility complex|Major histocompatibility complex]]
*[[MHC 3D structures|MHC 3D structures]]
*[[MHC II 3D structures|MHC II 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Corper, A L]]
[[Category: Corper AL]]
[[Category: Teyton, L]]
[[Category: Teyton L]]
[[Category: Wilson, I A]]
[[Category: Wilson IA]]
[[Category: Yoshida, K]]
[[Category: Yoshida K]]
[[Category: Glycoprotein]]
[[Category: Histocompatability antigen]]
[[Category: I-ag7]]
[[Category: Immune response]]
[[Category: Immune system]]
[[Category: Membrane]]
[[Category: Mhc class ii]]
[[Category: Mhc ii]]
[[Category: Transmembrane]]

Latest revision as of 10:54, 9 October 2024

Crystal structure of the MHC class II molecule I-Ag7 in complex with the peptide GAD221-235Crystal structure of the MHC class II molecule I-Ag7 in complex with the peptide GAD221-235

Structural highlights

3cup is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.09Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DCE2_RAT Catalyzes the production of GABA.[1] Q31135_MOUSE

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. ↑ Namchuk M, Lindsay L, Turck CW, Kanaani J, Baekkeskov S. Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65alpha. J Biol Chem. 1997 Jan 17;272(3):1548-57. PMID:8999827 doi:10.1074/jbc.272.3.1548

3cup, resolution 3.09Å

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