Literature summary for 3.4.14.4 extracted from

Bezerra, G.A.; Dobrovetsky, E.; Viertlmayr, R.; Dong, A.; Binter, A.; Abramic, M.; Macheroux, P.; Dhe-Paganon, S.; Gruber, K.
Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III (2012), Proc. Natl. Acad. Sci. USA, 109, 6525-6530.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of human DPP III and its complex with the opioid peptide tynorphin, to 1.8 A and 2.4 and.0 A resolution, respectively. Structures rationalize the enzymes substrate specificity and reveal an exceptionally large domain motion upon ligand binding. Microcalorimetric analyses point at an entropy-dominated process, with the release of water molecules from the binding cleft as the major thermodynamic driving force	Homo sapiens

Crystallization (Comment)

Organism

structures of human DPP III and its complex with the opioid peptide tynorphin, to 1.8 A and 2.4 and.0 A resolution, respectively. Structures rationalize the enzymes substrate specificity and reveal an exceptionally large domain motion upon ligand binding. Microcalorimetric analyses point at an entropy-dominated process, with the release of water molecules from the binding cleft as the major thermodynamic driving force

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9NY33	-	-

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Release 2023.1 (January 2023)