Location and nature of the residues important for ligand recognition in G-protein coupled receptors
(2005) In Journal of Molecular Recognition 18(1). p.60-72- Abstract
- The overall structure of the biogenic amine subclass of the G-protein-coupled receptors, and of their ligand binding sites, is discussed with the aim of highlighting the major structural features of these receptors that are responsible for ligand recognition. A comparison is made between biogenic amine receptors, peptide receptors of the rhodopsin class, and the secretin receptors which all have peptide ligands. The question of where the peptide ligands bind, whether at extracellular sites or within the transmembrane helix bundle, is discussed. The suitability of the rhodopsin crystal structure as a template for construction of homology models is discussed and it is concluded that there are many reasons why a caution should be issued... (More)
- The overall structure of the biogenic amine subclass of the G-protein-coupled receptors, and of their ligand binding sites, is discussed with the aim of highlighting the major structural features of these receptors that are responsible for ligand recognition. A comparison is made between biogenic amine receptors, peptide receptors of the rhodopsin class, and the secretin receptors which all have peptide ligands. The question of where the peptide ligands bind, whether at extracellular sites or within the transmembrane helix bundle, is discussed. The suitability of the rhodopsin crystal structure as a template for construction of homology models is discussed and it is concluded that there are many reasons why a caution should be issued against using it uncritically. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/249921
- author
- Bywater, Robert P. LU
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- ligand binding site, ligand binding residue, receptor, GPCR, antitarget, target
- in
- Journal of Molecular Recognition
- volume
- 18
- issue
- 1
- pages
- 60 - 72
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000227612900004
- scopus:11244255332
- pmid:15386622
- ISSN
- 1099-1352
- DOI
- 10.1002/jmr.685
- language
- English
- LU publication?
- yes
- id
- 84086829-5b80-447b-98e7-1a0bf610a718 (old id 249921)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=15386622&dopt=Abstract
- date added to LUP
- 2016-04-01 12:13:39
- date last changed
- 2022-01-27 00:44:05
@article{84086829-5b80-447b-98e7-1a0bf610a718,
abstract = {{The overall structure of the biogenic amine subclass of the G-protein-coupled receptors, and of their ligand binding sites, is discussed with the aim of highlighting the major structural features of these receptors that are responsible for ligand recognition. A comparison is made between biogenic amine receptors, peptide receptors of the rhodopsin class, and the secretin receptors which all have peptide ligands. The question of where the peptide ligands bind, whether at extracellular sites or within the transmembrane helix bundle, is discussed. The suitability of the rhodopsin crystal structure as a template for construction of homology models is discussed and it is concluded that there are many reasons why a caution should be issued against using it uncritically.}},
author = {{Bywater, Robert P.}},
issn = {{1099-1352}},
keywords = {{ligand binding site; ligand binding residue; receptor; GPCR; antitarget; target}},
language = {{eng}},
number = {{1}},
pages = {{60--72}},
publisher = {{John Wiley & Sons Inc.}},
series = {{Journal of Molecular Recognition}},
title = {{Location and nature of the residues important for ligand recognition in G-protein coupled receptors}},
url = {{http://dx.doi.org/10.1002/jmr.685}},
doi = {{10.1002/jmr.685}},
volume = {{18}},
year = {{2005}},
}