Skip to main content

Met-204 And Tyr-205 Are Together Important For Binding Glp-1 Receptor Agonists But Not Their N-Terminally Truncated Analogues

Buy Article:

$63.00 plus tax (Refund Policy)

Abstract:

A mutagenesis study to systematically analyse residues spanning the first extracellular loop of the GLP-1 receptor identified a double mutant, Met-204 / Tyr-205-Ala / Ala, which displayed: markedly reduced affinity for the natural agonist GLP-1; slightly reduced affinity for its analogue exendin-4; and unaltered affinity for several N-terminally truncated analogues of GLP-1 and exendin-4. This suggests that the locus is important for the formation of the binding site for the N-terminal residues of peptide agonists.

Keywords: Glp-1 Receptor; Met-204 And Tyr-205; N-terminally

Document Type: Review Article

DOI: https://doi.org/10.2174/0929866043478491

Affiliations: Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK

Publication date: 2004-02-01

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more