1u34: Difference between revisions

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New page: left|200px<br /><applet load="1u34" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u34" /> '''3D NMR structure of the first extracellular ...
 
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[[Image:1u34.gif|left|200px]]<br /><applet load="1u34" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1u34.gif|left|200px]]<br /><applet load="1u34" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1u34" />
caption="1u34" />
'''3D NMR structure of the first extracellular domain of CRFR-2beta, a type B1 G-protein coupled receptor'''<br />
'''3D NMR structure of the first extracellular domain of CRFR-2beta, a type B1 G-protein coupled receptor'''<br />


==Overview==
==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.
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==
==About this Structure==
1U34 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U34 OCA].  
1U34 is a [http://en.wikipedia.org/wiki/Single_protein 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==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: DiGruccio, M.R.]]
[[Category: DiGruccio, M R.]]
[[Category: Grace, C.R.]]
[[Category: Grace, C R.]]
[[Category: Miller, C.L.]]
[[Category: Miller, C L.]]
[[Category: Perrin, M.H.]]
[[Category: Perrin, M H.]]
[[Category: Riek, R.]]
[[Category: Riek, R.]]
[[Category: Rivier, J.E.]]
[[Category: Rivier, J E.]]
[[Category: Vale, W.W.]]
[[Category: Vale, W W.]]
[[Category: beta sheets and loops]]
[[Category: beta sheets and loops]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:48:54 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:08 2008''

Revision as of 13:20, 21 February 2008

File:1u34.gif


1u34

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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

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