Induced fit for mRNA/TIS11d complex.
TIS11d tandem zinc finger (TZF) domain can bind the class II AU-rich element of target mRNA and regulate mRNA turnover by promoting or inhibiting degradation. NMR spectra show that TIS11d(TZF) undergoes a transition from disordered to well folded upon binding to Zn and mRNA. To gain an insight into the mechanism, we have performed explicit-solvent molecular dynamics simulations (MD) for both bound and apo-TIS11d(TZF) to study the interdependence of binding and folding in the mRNA-TIS11d(TZF) complex. These results are in qualitative agreement with NMR experiment. Furthermore, this method could be used to other study about protein folding upon ligand binding.
Qin
Fang
F
College of Life Sciences and Biotechnology, Shanghai Jiaotong University, 800 Dongchuan Road, Shanghai 200240, China.
Chen
Yue
Y
Li
Yi-Xue
YX
Chen
Hai-Feng
HF
D020413:3' Untranslated Regions / Q000502:physiology; D000818:Animals; D001665:Binding Sites; D003198:Computer Simulation; D005260:Female; D019906:Nuclear Magnetic Resonance, Biomolecular; D009690:Nucleic Acid Conformation; D011485:Protein Binding / Q000235:genetics*; D011487:Protein Conformation; D017510:Protein Folding; D012333:RNA, Messenger / Q000378:metabolism*; D055672:Static Electricity; D013329:Structure-Activity Relationship; D015533:Transcriptional Activation; D016335:Zinc Fingers / Q000235:genetics* / Q000502:physiology
D020413:3' Untranslated Regions; D012333:RNA, Messenger