2jm4
From Proteopedia
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| - | [[Image:2jm4.jpg|left|200px]] | + | [[Image:2jm4.jpg|left|200px]] |
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| - | '''The solution NMR structure of the relaxin (RXFP1) receptor LDLa module.''' | + | {{Structure |
| + | |PDB= 2jm4 |SIZE=350|CAPTION= <scene name='initialview01'>2jm4</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= RXFP1, LGR7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''The solution NMR structure of the relaxin (RXFP1) receptor LDLa module.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2JM4 is a [ | + | 2JM4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JM4 OCA]. |
==Reference== | ==Reference== | ||
| - | The NMR solution structure of the relaxin (RXFP1) receptor lipoprotein receptor class A module and identification of key residues in the N-terminal region of the module that mediate receptor activation., Hopkins EJ, Layfield S, Ferraro T, Bathgate RA, Gooley PR, J Biol Chem. 2007 Feb 9;282(6):4172-84. Epub 2006 Dec 4. PMID:[http:// | + | The NMR solution structure of the relaxin (RXFP1) receptor lipoprotein receptor class A module and identification of key residues in the N-terminal region of the module that mediate receptor activation., Hopkins EJ, Layfield S, Ferraro T, Bathgate RA, Gooley PR, J Biol Chem. 2007 Feb 9;282(6):4172-84. Epub 2006 Dec 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17148455 17148455] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rxfp1 receptor]] | [[Category: rxfp1 receptor]] | ||
| - | ''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 17:42:44 2008'' |
Revision as of 15:42, 20 March 2008
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| Ligands: | |||||||
| Gene: | RXFP1, LGR7 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The solution NMR structure of the relaxin (RXFP1) receptor LDLa module.
Overview
The receptors for the peptide hormones relaxin and insulin-like peptide 3 (INSL3) are the leucine-rich repeat-containing G-protein-coupled receptors LGR7 and LGR8 recently renamed as the relaxin family peptide (RXFP) receptors, RXFP1 and RXFP2, respectively. These receptors differ from other LGRs by the addition of an N-terminal low density lipoprotein receptor class A (LDLa) module and are the only human G-protein-coupled receptors to contain such a domain. Recently it was shown that the LDLa module of the RXFP1 and RXFP2 receptors is essential for ligand-stimulated cAMP signaling. The mechanism by which the LDLa module modulates receptor signaling is unknown; however, it represents a unique paradigm in understanding G-protein-coupled receptor signaling. Here we present the structure of the RXFP1 receptor LDLa module determined by solution NMR spectroscopy. The structure is similar to other LDLa modules but shows small differences in side chain orientations and inter-residue packing. Interchange of the module with the second ligand binding domain of the LDL receptor, LB2, results in a receptor that binds relaxin with full affinity but is unable to signal. Furthermore, we demonstrate via structural studies on mutated LDLa modules and functional studies on mutated full-length receptors that a hydrophobic surface within the N-terminal region of the module is essential for activation of RXFP1 receptor signal in response to relaxin stimulation. This study has highlighted the necessity to understand the structural effects of single amino acid mutations on the LDLa module to fully interpret the effects of these mutations on receptor activity.
About this Structure
2JM4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The NMR solution structure of the relaxin (RXFP1) receptor lipoprotein receptor class A module and identification of key residues in the N-terminal region of the module that mediate receptor activation., Hopkins EJ, Layfield S, Ferraro T, Bathgate RA, Gooley PR, J Biol Chem. 2007 Feb 9;282(6):4172-84. Epub 2006 Dec 4. PMID:17148455
Page seeded by OCA on Thu Mar 20 17:42:44 2008
