Molecular mechanics study of ion binding by a cyclic pentapeptide.
We have used energy minimization and harmonic analysis to study the structural and thermodynamic changes which occur upon the binding of lithium ions to the cyclic pentapeptide, cyclo-(Gly-L-Pro-Gly-D-Ala-L-Pro) (GPGAP). A number of theoretically stable vacuum configurations of uncomplexed GPGAP were found, one of which is very close to the crystal conformation determined by X-ray diffraction. Stable complexes with lithium were found where the ion binds to the carbonyl oxygen atoms of three residues. Detailed conformational information is presented for both the uncomplexed and the complexed peptide, along with an analysis of the atomic interactions which stabilize the various peptide conformations.
D001665:Binding Sites; D007476:Ionophores; D008094:Lithium / Q000378:metabolism*; D008958:Models, Molecular; D010456:Peptides, Cyclic / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013816:Thermodynamics
D007476:Ionophores; D010456:Peptides, Cyclic; D008094:Lithium