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1u34

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Revision as of 09:35, 29 September 2021

3D NMR structure of the first extracellular domain of CRFR-2beta, a type B1 G-protein coupled receptor

Structural highlights

1u34 is a 1 chain structure with sequence from Lk3 transgenic mice. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CRFR2_MOUSE] This is a receptor for corticotropin releasing factor. Shows high-affinity CRF binding. Also binds to urocortin I, II and III. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.

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

The corticotropin-releasing factor (CRF) ligand family has diverse effects on the CNS, including the modulation of the stress response. The ligands' effects are mediated by binding to CRF G protein-coupled receptors. We have determined the 3D NMR structure of the N-terminal extracellular domain (ECD1) of the mouse CRF receptor 2beta, which is the major ligand recognition domain, and identified its ligand binding site by chemical-shift perturbation experiments. The fold is identified as a short consensus repeat (SCR), a common protein interaction module. Mutagenesis reveals the integrity of the hormone-binding site in the full-length receptor. This study proposes that the ECD1 captures the C-terminal segment of the ligand, whose N terminus then penetrates into the transmembrane region of the receptor to initiate signaling. Key residues of SCR in the ECD1 are conserved in the G protein-coupled receptor subfamily, suggesting the SCR fold in all of the ECD1s of this subfamily.

NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor.,Grace CR, Perrin MH, DiGruccio MR, Miller CL, Rivier JE, Vale WW, Riek R Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12836-41. Epub 2004 Aug 23. PMID:15326300^[1]

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

References

↑ Grace CR, Perrin MH, DiGruccio MR, Miller CL, Rivier JE, Vale WW, Riek R. NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor. Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12836-41. Epub 2004 Aug 23. PMID:15326300 doi:10.1073/pnas.0404702101

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u34"

@@ Line 3: / Line 3: @@
 <StructureSection load='1u34' size='340' side='right'caption='[[1u34]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1u34]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U34 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U34 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1u34]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U34 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=1u34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u34 OCA], [http://pdbe.org/1u34 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u34 RCSB], [http://www.ebi.ac.uk/pdbsum/1u34 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u34 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=1u34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u34 OCA], [https://pdbe.org/1u34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u34 RCSB], [https://www.ebi.ac.uk/pdbsum/1u34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u34 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CRFR2_MOUSE CRFR2_MOUSE]] This is a receptor for corticotropin releasing factor. Shows high-affinity CRF binding. Also binds to urocortin I, II and III. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
+[[https://www.uniprot.org/uniprot/CRFR2_MOUSE CRFR2_MOUSE]] This is a receptor for corticotropin releasing factor. Shows high-affinity CRF binding. Also binds to urocortin I, II and III. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1u34

From Proteopedia

Revision as of 09:35, 29 September 2021

3D NMR structure of the first extracellular domain of CRFR-2beta, a type B1 G-protein coupled receptor

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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