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Search results 201 to 215 out of 215 for Ghrhr

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0.019s

Type

Details

Score

Publication

33060564 | -

First Author:	Zhou F
Year:	2020
Journal:	Nat Commun
Title:	Structural basis for activation of the growth hormone-releasing hormone receptor.
Volume:	11
Issue:	1
Pages:	5205

•

Protein Domain

IPR003288 | GPCR_2_GHRH_rcpt

Type:

Family

Description:

G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups []. The term clan can be used to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence []. The currently known clan members include rhodopsin-like GPCRs (Class A, GPCRA), secretin-like GPCRs (Class B, GPCRB), metabotropic glutamate receptor family (Class C, GPCRC), fungal mating pheromone receptors (Class D, GPCRD), cAMP receptors (Class E, GPCRE) and frizzled/smoothened (Class F, GPCRF) [, , , , ]. GPCRs are major drug targets, and are consequently the subject of considerable research interest. It has been reported that the repertoire of GPCRs for endogenous ligands consists of approximately 400 receptors in humans and mice []. Most GPCRs are identified on the basis of their DNA sequences, rather than the ligand they bind, those that are unmatched to known natural ligands are designated by as orphan GPCRs, or unclassified GPCRs [].The secretin-like GPCRs include secretin [], calcitonin [], parathyroid hormone/parathyroid hormone-related peptides []and vasoactive intestinal peptide [], all of which activate adenylyl cyclase and the phosphatidyl-inositol-calcium pathway. These receptors contain seven transmembrane regions, in a manner reminiscent of the rhodopsins and other receptors believed to interact with G-proteins (however there is no significant sequence identity between these families, the secretin-like receptors thus bear their own unique '7TM' signature). Their N-terminal is probably located on the extracellular side of the membrane and potentially glycosylated. This N-terminal region contains a long conserved region which allows the binding of large peptidic ligand such as glucagon, secretin, VIP and PACAP; this region contains five conserved cysteines residues which could be involved in disulphide bond. The C-terminal region of these receptor is probably cytoplasmic. Every receptor gene in this family is encoded on multiple exons, and several of these genes are alternatively spliced to yield functionally distinct products. Growth hormone (GH)-releasing hormone (GHRH) belongs to the family of gut-neuropeptide hormones that includes glucagon, secretin and vasoactive intestinal peptide (VIP) []. The receptors for this peptide family involve similar signal transduction pathways - on hormone binding, they interact with G protein and cause stimulation of adenylate cyclase []. Acting through the GHRH receptor (GHRHR), GH plays a pivotal role in the regulation of GH synthesis and secretion in the pituitary, possibly serving other roles in different tissues []. Cryo-electron microscopy shows a hormone recognition pattern where an α-helical GHRH forms interactions involving all the extracellular loops, most TM helices, and a linker from GHRHR []. The human pituitary GHRHR is a 423-amino acid protein that has the characteristic 7TM signature of the secretin-like GPCR superfamily, sharing 47%, 42%, 35%, and 28% identity with receptors for VIP, secretin, calcitonin and PTH, respectively [].

•

Protein

P32082

Organism:	Mus musculus/domesticus
Length:	423
Fragment?:	false

•

Protein

A0A0N4SVS4

Organism:	Mus musculus/domesticus
Length:	386
Fragment?:	false

•

Publication

1646711 | -

First Author:	Ishihara T
Year:	1991
Journal:	EMBO J
Title:	Molecular cloning and expression of a cDNA encoding the secretin receptor.
Volume:	10
Issue:	7
Pages:	1635-41

•

Publication

1314625 | -

First Author:	Ishihara T
Year:	1992
Journal:	Neuron
Title:	Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide.
Volume:	8
Issue:	4
Pages:	811-9

•

Publication

1658940 | -

First Author:	Lin HY
Year:	1991
Journal:	Science
Title:	Expression cloning of an adenylate cyclase-coupled calcitonin receptor.
Volume:	254
Issue:	5034
Pages:	1022-4

•

Publication

1658941 | -

First Author:	Jüppner H
Year:	1991
Journal:	Science
Title:	A G protein-linked receptor for parathyroid hormone and parathyroid hormone-related peptide.
Volume:	254
Issue:	5034
Pages:	1024-6

•

Publication

12679517 | J:83410

First Author:	Vassilatis DK
Year:	2003
Journal:	Proc Natl Acad Sci U S A
Title:	The G protein-coupled receptor repertoires of human and mouse.
Volume:	100
Issue:	8
Pages:	4903-8

•

Publication

8170923 | -

First Author:	Attwood TK
Year:	1994
Journal:	Protein Eng
Title:	Fingerprinting G-protein-coupled receptors.
Volume:	7
Issue:	2
Pages:	195-203

•

Publication

8081729 | -

First Author:	Kolakowski LF Jr
Year:	1994
Journal:	Receptors Channels
Title:	GCRDb: a G-protein-coupled receptor database.
Volume:	2
Issue:	1
Pages:	1-7

•

Publication

15914470 | -

First Author:	Foord SM
Year:	2005
Journal:	Pharmacol Rev
Title:	International Union of Pharmacology. XLVI. G protein-coupled receptor list.
Volume:	57
Issue:	2
Pages:	279-88

•

Publication

18948278 | -

First Author:	Harmar AJ
Year:	2009
Journal:	Nucleic Acids Res
Title:	IUPHAR-DB: the IUPHAR database of G protein-coupled receptors and ion channels.
Volume:	37
Issue:	Database issue
Pages:	D680-5

•

Publication

16753280 | J:115055

First Author:	Bjarnadóttir TK
Year:	2006
Journal:	Genomics
Title:	Comprehensive repertoire and phylogenetic analysis of the G protein-coupled receptors in human and mouse.
Volume:	88
Issue:	3
Pages:	263-73

•

Publication

23020293 | -

First Author:	Civelli O
Year:	2013
Journal:	Annu Rev Pharmacol Toxicol
Title:	G protein-coupled receptor deorphanizations.
Volume:	53

Pages:	127-46

•

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