2001
DOI: 10.1021/bi001758y
|View full text |Cite
|
Sign up to set email alerts
|

Juxtamembrane Region of the Amino Terminus of the Corticotropin Releasing Factor Receptor Type 1 Is Important for Ligand Interaction

Abstract: The functional properties of the amino terminus (NT) of the corticotropin releasing factor (CRF) receptor type 1 (R1) were studied by use of murine (m) CRFR1 and rat (r) parathyroid hormone (PTH)/parathyroid hormone-related peptide receptor (PTH1R) chimeras. The chimeric receptor CXP, in which the NT of mCRFR1 was annealed to the TMs of PTH1R, and the reciprocal hybrid, PXC, bound radiolabeled analogues of sauvagine and PTH(3--34), respectively. Neither hybrid bound radiolabeled CRF or PTH(1--34). CRF and PTH(… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

2
33
0
1

Year Published

2002
2002
2016
2016

Publication Types

Select...
6
3

Relationship

0
9

Authors

Journals

citations
Cited by 37 publications
(36 citation statements)
references
References 45 publications
2
33
0
1
Order By: Relevance
“…Statistically significant differences between the logEC 50 values of wild-type and mutant receptors were evaluated using one-way analysis of variance followed by Bonferoni's post hoc test ‫,ء(‬ p Ͻ 0.05). molpharm.aspetjournals.org bind differentially to CRF 1 has also been suggested in a previous study, in which the pharmacological properties of different peptides were differentially affected by several mutations of receptor (Assil et al, 2001).…”
Section: Discussionsupporting
confidence: 64%
“…Statistically significant differences between the logEC 50 values of wild-type and mutant receptors were evaluated using one-way analysis of variance followed by Bonferoni's post hoc test ‫,ء(‬ p Ͻ 0.05). molpharm.aspetjournals.org bind differentially to CRF 1 has also been suggested in a previous study, in which the pharmacological properties of different peptides were differentially affected by several mutations of receptor (Assil et al, 2001).…”
Section: Discussionsupporting
confidence: 64%
“…CRF receptors are predicted to consist of a large extracellular N-terminal domain (N-domain), connected to the juxtamembrane region consisting of the transmembrane domains and intervening loops (J-domain) (Perrin and Vale, 1999;Grigoriadis et al, 2001). The N-domain is a determinant of high-affinity peptide ligand binding (Liaw et al, 1997b;Dautzenberg et al, 1998;Perrin et al, 1998;Wille et al, 1999;Assil et al, 2001;Hofmann et al, 2001;Perrin et al, 2001). Regions and residues in the J-domain are involved in receptor activation by peptide ligands Nielsen et al, 2000;Assil et al, 2001) and contribute to ligand binding affinity (Liaw et al, 1997a,b;Perrin et al, 1998;Sydow et al, 1999).…”
Section: Celerated [mentioning
confidence: 99%
“…The N-domain is a determinant of high-affinity peptide ligand binding (Liaw et al, 1997b;Dautzenberg et al, 1998;Perrin et al, 1998;Wille et al, 1999;Assil et al, 2001;Hofmann et al, 2001;Perrin et al, 2001). Regions and residues in the J-domain are involved in receptor activation by peptide ligands Nielsen et al, 2000;Assil et al, 2001) and contribute to ligand binding affinity (Liaw et al, 1997a,b;Perrin et al, 1998;Sydow et al, 1999). Collectively, these results suggest that the N-terminal portion of the ligand binds the J-domain of the receptor (for activation), and the C-terminal ligand region binds the receptor's N-domain (for high-affinity binding).…”
Section: Celerated [mentioning
confidence: 99%
“…Understanding hormone-PTH1R and PTH1R-G protein interactions has relied largely on determination of functional consequences resulting from mutations in either the hormone or the receptor (13,(22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35)(36), analysis of receptor fragments after cross-linking to radioiodinated, p-benzoyl-L-phenylalaninemodified ligands (13,(37)(38)(39)(40), crystallographic resolution of PTH (41), and NMR of PTH (42)(43)(44)(45)(46)(47)(48)(49)(50)(51)(52)(53)(54)(55)(56)(57)(58), PTHrP (59 -68), and short segments of the PTH1R (see Refs. 69 and 70 and for review see Refs.…”
Section: The Parathyroid Hormone (Pth)mentioning
confidence: 99%