Structural insights of the MLF1/14‐3‐3 interaction

Myeloid leukaemia factor 1 (MLF1) binds to 14‐3‐3 adapter proteins by a sequence surrounding Ser34 with the functional consequences of this interaction largely unknown. We present here the high‐resolution crystal structure of this binding motif [MLF1(29–42)pSer34] in complex with 14‐3‐3ε and analyse...

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Veröffentlicht in:	The FEBS journal 2012-02, Vol.279 (4), p.563-571
Hauptverfasser:	Molzan, Manuela, Weyand, Michael, Rose, Rolf, Ottmann, Christian
Format:	Artikel
Sprache:	eng
Schlagworte:	14-3-3 Proteins - chemistry 14-3-3 Proteins - genetics 14-3-3 Proteins - metabolism Amino Acid Motifs - genetics Amino Acid Sequence Binding Sites - genetics Calorimetry - methods Crystal structure Crystallography, X-Ray drug discovery fragment‐based ligand discovery Humans Hydrogen Bonding Hydrophobic and Hydrophilic Interactions leukaemia Leukemia Models, Molecular Molecular biology Molecular Sequence Data Peptide Fragments - chemistry Peptide Fragments - metabolism PPI stabilization Protein Structure, Tertiary Proteins Proteins - chemistry Proteins - genetics Proteins - metabolism protein–protein interactions Recombinant Proteins - chemistry Recombinant Proteins - metabolism Serine - chemistry Serine - genetics Serine - metabolism X‐ray crystallography
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