2N0I

NMR solution structure for di-sulfide 11mer peptide

Summary for 2N0I

• Entry DOI: 10.2210/pdb2n0i/pdb
• Related: 2N08 2N09 2N0N
• NMR Information: BMRB: 26538
• Descriptor: di-sulfide 11mer peptide (1 entity in total)
• Functional Keywords: de novo protein
• Total number of polymer chains: 1
• Total formula weight: 1347.52

Authors

Hoang, H.N.,Song, K.,Hill, T.A.,Derksen, D.R.,Edmonds, D.J.,Kok, W.M.,Limberakis, C.,Liras, S.,Loria, P.M.,Mascitti, V.,Mathiowetz, A.M.,Mitchell, J.M.,Piotrowski, D.W.,Price, D.A.,Stanton, R.V.,Suen, J.Y.,Withka, J.M.,Griffith, D.A.,Fairlie, D.P. (deposition date: 2015-03-09, release date: 2015-04-15, Last modification date: 2024-04-03)

Primary citation

Hoang, H.N.,Song, K.,Hill, T.A.,Derksen, D.R.,Edmonds, D.J.,Kok, W.M.,Limberakis, C.,Liras, S.,Loria, P.M.,Mascitti, V.,Mathiowetz, A.M.,Mitchell, J.M.,Piotrowski, D.W.,Price, D.A.,Stanton, R.V.,Suen, J.Y.,Withka, J.M.,Griffith, D.A.,Fairlie, D.P.
Short Hydrophobic Peptides with Cyclic Constraints Are Potent Glucagon-like Peptide-1 Receptor (GLP-1R) Agonists.
J.Med.Chem., 58:4080-4085, 2015

PubMed 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 β-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.

PubMed: 25839426
DOI: 10.1021/acs.jmedchem.5b00166

Experimental method

SOLUTION NMR