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Specificity of the thrombin receptor for agonist peptide is defined by its extracellular surface

Nature (London), 1994-04, Vol.368 (6472), p.648-651 [Peer Reviewed Journal]

1994 INIST-CNRS ;Copyright Macmillan Journals Ltd. Apr 14, 1994 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/368648a0 ;PMID: 8145852 ;CODEN: NATUAS

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Title:
Specificity of the thrombin receptor for agonist peptide is defined by its extracellular surface
Author: Gerszten, Robert E ; Chen, Ji ; Ishli, Maki ; Ishil, Kenji ; Wang, Ling ; Nanevicz, Tania ; Turck, Christoph W ; Vu, Thien-Khai H ; Coughlin, Shaun R
Subjects: Amino Acid Sequence ; Animals ; Biological and medical sciences ; Cell Line ; Cell receptors ; Cell structures and functions ; Cellular biology ; Fundamental and applied biological sciences. Psychology ; Humans ; Ligands ; Miscellaneous ; Molecular and cellular biology ; Molecular Sequence Data ; Peptide Fragments - metabolism ; Peptide hormones ; Proteins ; Rats ; Receptors ; Receptors, Thrombin - metabolism ; Recombinant Fusion Proteins - metabolism ; Sequence Homology, Amino Acid ; Structure-Activity Relationship ; Thrombin ; Xenopus
Is Part Of: Nature (London), 1994-04, Vol.368 (6472), p.648-651
Description: G-protein-coupled receptors for catecholamines and some other small ligands are activated when agonists bind to the transmembrane region of the receptor. The docking interactions through which peptide agonists activate their receptors are less well characterized. The thrombin receptor is a specialized peptide receptor. It is activated by binding its tethered ligand domain, which is unmasked upon receptor cleavage by thrombin. Human and Xenopus thrombin receptor homologues are each selectively activated by the agonist peptide representing their respective tethered ligand domains. Here we identify receptor domains that confer this agonist specificity by replacing the Xenopus receptor's aminoterminal exodomain and three extracellular loops with the corresponding human structures. This switches receptor specificity from Xenopus to human. The specificity of these thrombin receptors for their respective peptide agonists is thus determined by their extracellular surfaces. Our results indicate that agonist interaction with extracellular domains is important for thrombin receptor activation.
Publisher: London: Nature Publishing
Language: English
Identifier: ISSN: 0028-0836
EISSN: 1476-4687
DOI: 10.1038/368648a0
PMID: 8145852
CODEN: NATUAS
Source: ProQuest One Psychology
AUTh Library subscriptions: ProQuest Central
MEDLINE
Alma/SFX Local Collection

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Specificity of the thrombin receptor for agonist peptide is defined by its extracellular surface

1994 INIST-CNRS ;Copyright Macmillan Journals Ltd. Apr 14, 1994 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/368648a0 ;PMID: 8145852 ;CODEN: NATUAS

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