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1es0

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Revision as of 09:50, 26 May 2021

CRYSTAL STRUCTURE OF THE MURINE CLASS II ALLELE I-A(G7) COMPLEXED WITH THE GLUTAMIC ACID DECARBOXYLASE (GAD65) PEPTIDE 207-220

Structural highlights

1es0 is a 2 chain structure with sequence from Human and Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DCE2_HUMAN] Catalyzes the production of GABA.

Evolutionary Conservation

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

Publication Abstract from PubMed

Susceptibility to murine and human insulin-dependent diabetes mellitus correlates strongly with major histocompatibility complex (MHC) class II I-A or HLA-DQ alleles that lack an aspartic acid at position beta57. I-Ag7 lacks this aspartate and is the only class II allele expressed by the nonobese diabetic mouse. The crystal structure of I-Ag7 was determined at 2.6 angstrom resolution as a complex with a high-affinity peptide from the autoantigen glutamic acid decarboxylase (GAD) 65. I-Ag7 has a substantially wider peptide-binding groove around beta57, which accounts for distinct peptide preferences compared with other MHC class II alleles. Loss of Asp(beta57) leads to an oxyanion hole in I-Ag7 that can be filled by peptide carboxyl residues or, perhaps, through interaction with the T cell receptor.

A structural framework for deciphering the link between I-Ag7 and autoimmune diabetes.,Corper AL, Stratmann T, Apostolopoulos V, Scott CA, Garcia KC, Kang AS, Wilson IA, Teyton L Science. 2000 Apr 21;288(5465):505-11. PMID:10775108^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Corper AL, Stratmann T, Apostolopoulos V, Scott CA, Garcia KC, Kang AS, Wilson IA, Teyton L. A structural framework for deciphering the link between I-Ag7 and autoimmune diabetes. Science. 2000 Apr 21;288(5465):505-11. PMID:10775108

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1es0"

@@ Line 3: / Line 3: @@
 <StructureSection load='1es0' size='340' side='right'caption='[[1es0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1es0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ES0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ES0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1es0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ES0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ES0 FirstGlance]. <br>
-</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=1es0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1es0 OCA], [http://pdbe.org/1es0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1es0 RCSB], [http://www.ebi.ac.uk/pdbsum/1es0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1es0 ProSAT]</span></td></tr>
+</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=1es0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1es0 OCA], [https://pdbe.org/1es0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1es0 RCSB], [https://www.ebi.ac.uk/pdbsum/1es0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1es0 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DCE2_HUMAN DCE2_HUMAN]] Catalyzes the production of GABA.
+[[https://www.uniprot.org/uniprot/DCE2_HUMAN DCE2_HUMAN]] Catalyzes the production of GABA.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 29: @@
 ==See Also==
-*[[Major histocompatibility complex|Major histocompatibility complex]]
+*[[MHC 3D structures|MHC 3D structures]]
 == References ==
 <references/>

1es0

From Proteopedia

Revision as of 09:50, 26 May 2021

CRYSTAL STRUCTURE OF THE MURINE CLASS II ALLELE I-A(G7) COMPLEXED WITH THE GLUTAMIC ACID DECARBOXYLASE (GAD65) PEPTIDE 207-220

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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