 |
PDBsum entry 5u3a
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
|
|
Title
|
|
Folding then binding vs folding through binding in macrocyclic peptide inhibitors of human pancreatic α-Amylase.
|
|
|
Authors
|
|
L.Goldbach,
B.J.A.Vermeulen,
S.Caner,
M.Liu,
C.Tysoe,
L.Van gijzel,
R.Yoshisada,
M.Trellet,
H.Van ingen,
G.D.Brayer,
A.M.J.J.Bonvin,
S.A.K.Jongkees.
|
|
|
Ref.
|
|
ACS Chem Biol, 2019,
14,
1751-1759.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
De novo macrocyclic peptides, derived using selection technologies such
as phage and mRNA display, present unique and unexpected solutions to
challenging biological problems. This is due in part to their unusual folds,
which are able to present side chains in ways not available to canonical
structures such as α-helices and β-sheets. Despite much recent interest in
these molecules, their folding and binding behavior remains poorly
characterized. In this work, we present cocrystallization, docking, and solution
NMR structures of three de novo macrocyclic peptides that all bind as
competitive inhibitors with single-digit nanomolar K
|
|
|
|
|
|
|
