2N0I: NMR solution structure for di-sulfide 11mer peptide

Citation:
Abstract
Cyclic constraints are incorporated into an 11-residue analogue of the N-terminus of glucagon-like peptide-1 (GLP-1) to investigate effects of structure on agonist activity. Cyclization through linking side chains of residues 2 and 5 or 5 and 9 produced agonists at nM concentrations in a cAMP assay. 2D NMR and CD spectra revealed an N-terminal beta-turn and a C-terminal helix that differentially influenced affinity and agonist potency. These structures can inform development of small molecule agonists of the GLP-1 receptor to treat type 2 diabetes.
PDB ID: 2N0IDownload
MMDB ID: 128531
PDB Deposition Date: 2015/3/9
Updated in MMDB: 2018/05
Experimental Method:
solution nmr
Similar Structures:
Biological Unit for 2N0I: monomeric; determined by author
Molecular Components in 2N0I
Label Count Molecule
Protein (1 molecule)
1
Di-sulfide 11mer Peptide
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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