Structural Study of a Flexible Active Site Loop in Human Indoleamine 2,3-Dioxygenase and Its Functional Implications

Human indoleamine 2,3-dioxygenase catalyzes the oxidative cleavage of tryptophan to N-formyl kynurenine, the initial and rate-limiting step in the kynurenine pathway. Additionally, this enzyme has been identified as a possible target for cancer therapy. A 20-amino acid protein segment (the JK loop),...

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Detalles Bibliográficos
Autores principales: Álvarez, L., Lewis-Ballester, A., Roitberg, A., Estrin, D.A., Yeh, S.-R., Marti, M.A., Capece, L.
Formato: JOUR
Materias:
Amino acids
Binding energy
Bins
Catalysis
Conformations
Enzyme activity
Hydrogen bonds
Molecular dynamics
Mutagenesis
Proteins
Hydrogen bonding interactions
Indoleamine 2 ,3-dioxygenase
Post-translational modifications
Protein-protein interactions
Replica-exchange molecular dynamics simulations
Site directed mutagenesis
Structural rearrangement
Structure and dynamics
Crystal structure
indoleamine 2,3 dioxygenase
kynurenine
tryptophan
indoleamine 2,3-dioxygenase 1, human
Article
binding site
cancer therapy
catalyst
comparative study
conformational transition
crystal structure
enzyme activity
enzyme structure
human
hydrogen bond
molecular dynamics
priority journal
protein protein interaction
protein purification
protein secondary structure
signal transduction
site directed mutagenesis
static electricity
catalysis
chemistry
genetics
metabolism
protein domain
protein motif
structure activity relation
X ray crystallography
Amino Acid Motifs
Crystallography, X-Ray
Humans
Indoleamine-Pyrrole 2,3,-Dioxygenase
Mutagenesis, Site-Directed
Protein Domains
Structure-Activity Relationship
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00062960_v55_n19_p2785_Alvarez
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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