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 Lettjournal_title
FEBS lettersauthors
López de Maturana R,Donnelly Ddoi
10.1016/s0014-5793(02)03492-0keywords:
subject
Has Abstractpub_date
2002-10-23 00:00:00pages
244-8issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302034920journal_volume
530pub_type
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