5eh1: Difference between revisions

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'''Unreleased structure'''


The entry 5eh1 is ON HOLD until Paper Publication
==Crystal structure of the extracellular part of receptor 2 of human interferon gamma==
 
<StructureSection load='5eh1' size='340' side='right' caption='[[5eh1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5eh1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EH1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EH1 FirstGlance]. <br>
Description:  
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
[[Category: Unreleased Structures]]
<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=5eh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eh1 OCA], [http://pdbe.org/5eh1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eh1 RCSB], [http://www.ebi.ac.uk/pdbsum/5eh1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eh1 ProSAT]</span></td></tr>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/INGR2_HUMAN INGR2_HUMAN]] Autosomal recessive mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR2 deficiency;Autosomal dominant mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR2 deficiency;Mendelian susceptibility to mycobacterial diseases due to complete IFNgammaR2 deficiency. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[[http://www.uniprot.org/uniprot/INGR2_HUMAN INGR2_HUMAN]] Associates with IFNGR1 to form a receptor for the cytokine interferon gamma (IFNG) (PubMed:8124716, PubMed:7673114,PubMed:7615558). Ligand binding stimulates activation of the JAK/STAT signaling pathway (PubMed:8124716, PubMed:7673114, PubMed:15356148). Required for signal transduction in contrast to other receptor subunit responsible for ligand binding (PubMed:7673114).<ref>PMID:15356148</ref> <ref>PMID:7615558</ref> <ref>PMID:7673114</ref> <ref>PMID:8124716</ref>  
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cerny, J]]
[[Category: Coval, T]]
[[Category: Dohnalek, J]]
[[Category: Kolenko, P]]
[[Category: Mikulecky, P]]
[[Category: Necasova, I]]
[[Category: Schneider, B]]
[[Category: Zahradnik, J]]
[[Category: Cytokine]]
[[Category: Fibronectin iii domain]]
[[Category: Immunity]]
[[Category: Interferon gamma]]

Revision as of 03:01, 10 September 2016

Crystal structure of the extracellular part of receptor 2 of human interferon gammaCrystal structure of the extracellular part of receptor 2 of human interferon gamma

Structural highlights

5eh1 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[INGR2_HUMAN] Autosomal recessive mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR2 deficiency;Autosomal dominant mendelian susceptibility to mycobacterial diseases due to partial IFNgammaR2 deficiency;Mendelian susceptibility to mycobacterial diseases due to complete IFNgammaR2 deficiency. The disease is caused by mutations affecting the gene represented in this entry.

Function

[INGR2_HUMAN] Associates with IFNGR1 to form a receptor for the cytokine interferon gamma (IFNG) (PubMed:8124716, PubMed:7673114,PubMed:7615558). Ligand binding stimulates activation of the JAK/STAT signaling pathway (PubMed:8124716, PubMed:7673114, PubMed:15356148). Required for signal transduction in contrast to other receptor subunit responsible for ligand binding (PubMed:7673114).[1] [2] [3] [4]

References

  1. ↑ Rosenzweig SD, Schwartz OM, Brown MR, Leto TL, Holland SM. Characterization of a dipeptide motif regulating IFN-gamma receptor 2 plasma membrane accumulation and IFN-gamma responsiveness. J Immunol. 2004 Sep 15;173(6):3991-9. PMID:15356148
  2. ↑ Sakatsume M, Igarashi K, Winestock KD, Garotta G, Larner AC, Finbloom DS. The Jak kinases differentially associate with the alpha and beta (accessory factor) chains of the interferon gamma receptor to form a functional receptor unit capable of activating STAT transcription factors. J Biol Chem. 1995 Jul 21;270(29):17528-34. PMID:7615558
  3. ↑ Kotenko SV, Izotova LS, Pollack BP, Mariano TM, Donnelly RJ, Muthukumaran G, Cook JR, Garotta G, Silvennoinen O, Ihle JN, et al.. Interaction between the components of the interferon gamma receptor complex. J Biol Chem. 1995 Sep 8;270(36):20915-21. PMID:7673114
  4. ↑ Soh J, Donnelly RJ, Kotenko S, Mariano TM, Cook JR, Wang N, Emanuel S, Schwartz B, Miki T, Pestka S. Identification and sequence of an accessory factor required for activation of the human interferon gamma receptor. Cell. 1994 Mar 11;76(5):793-802. PMID:8124716

5eh1, resolution 1.80Å

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