Domain packing and dynamics in the DNA complex of the N-terminal zinc fingers of TFIIIA.
The three N-terminal zinc fingers of transcription factor IIIA bind in the DNA major groove. Substantial packing interfaces are formed between adjacent fingers, the linkers lose their intrinsic flexibility upon DNA binding, and several lysine side chains implicated in DNA recognition are dynamically disordered.
Foster
M P
MP
Wuttke
D S
DS
Radhakrishnan
I
I
Case
D A
DA
Gottesfeld
J M
JM
Wright
P E
PE
D000595:Amino Acid Sequence; D004247:DNA / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D008239:Lysine / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors / Q000737:chemistry*; D016335:Zinc Fingers
D004268:DNA-Binding Proteins; D010446:Peptide Fragments; D035582:Transcription Factor TFIIIA; D014157:Transcription Factors; D004247:DNA; D008239:Lysine