Phosphorylation regulates the bound structure of an intrinsically disordered protein: The p53-TAZ2 case

Disordered regions and Intrinsically Disordered Proteins (IDPs) are involved in critical cellular processes and may acquire a stable three-dimensional structure only upon binding to their partners. IDPs may follow a folding-after-binding process, known as induced folding, or a folding-before-binding...

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Detalles Bibliográficos
Autores principales: Ithuralde, R.E., Turjanski, A.G.
Formato: JOUR
Materias:
intrinsically disordered protein
protein p53
bone sialoprotein (35-62), human
peptide fragment
protein binding
sialoglycoprotein
Article
binding affinity
binding site
complex formation
controlled study
molecular recognition
protein determination
protein folding
protein phosphorylation
protein processing
protein protein interaction
structure analysis
chemistry
genetic transcription
genetics
human
metabolism
molecular dynamics
molecular genetics
phosphorylation
protein motif
protein secondary structure
protein tertiary structure
Amino Acid Motifs
Binding Sites
Humans
Intrinsically Disordered Proteins
Molecular Dynamics Simulation
Molecular Sequence Data
Peptide Fragments
Phosphorylation
Protein Binding
Protein Folding
Protein Processing, Post-Translational
Protein Structure, Secondary
Protein Structure, Tertiary
Sialoglycoproteins
Transcription, Genetic
Tumor Suppressor Protein p53
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_19326203_v11_n1_p_Ithuralde
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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