The glucagon-like peptide-1 receptor binding site for the N-terminus of GLP-1 requires polarity at Asp198 rather than negative charge.

Abstract:

:The mutation of Asp198 to Asn in the receptor for glucagon-like peptide-1(7-36)amide (GLP-1) had no effect upon GLP-1 affinity whereas substitution with Ala greatly reduced affinity, demonstrating the importance of polarity rather than negative charge at Asp198. However, the Asp198-Ala mutation had less effect upon the affinity of Exendin-4, a peptide agonist that has been shown previously not to require its N-terminus for high affinity. Moreover, the affinity of a truncated GLP-1 analogue lacking the first eight residues was not affected by the Asp198-Ala mutation, demonstrating that Asp198 is required for maintaining the binding site of the N-terminal region of GLP-1.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

López de Maturana R,Donnelly D

doi

10.1016/s0014-5793(02)03492-0

keywords:

subject

Has Abstract

pub_date

2002-10-23 00:00:00

pages

244-8

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579302034920

journal_volume

530

pub_type

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