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1u34
From Proteopedia
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| - | [[Image:1u34.gif|left|200px]] | + | [[Image:1u34.gif|left|200px]] |
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| - | '''3D NMR structure of the first extracellular domain of CRFR-2beta, a type B1 G-protein coupled receptor''' | + | {{Structure |
| + | |PDB= 1u34 |SIZE=350|CAPTION= <scene name='initialview01'>1u34</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''3D NMR structure of the first extracellular domain of CRFR-2beta, a type B1 G-protein coupled receptor''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1U34 is a [ | + | 1U34 is a [[Single protein]] structure of 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=1U34 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15326300 15326300] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Rivier, J E.]] | [[Category: Rivier, J E.]] | ||
[[Category: Vale, W W.]] | [[Category: Vale, W W.]] | ||
| - | [[Category: beta sheets and | + | [[Category: beta sheets and loop]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:26:45 2008'' |
Revision as of 12:26, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
3D NMR structure of the first extracellular domain of CRFR-2beta, a type B1 G-protein coupled receptor
Overview
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.
About this Structure
1U34 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 14:26:45 2008
