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.
College of Life Sciences and Biotechnology, Shanghai Jiaotong University, 800 Dongchuan Road, Shanghai 200240, China.
Fang
F
Qin
Yue
Y
Chen
Yi-Xue
YX
Li
Hai-Feng
HF
Chen
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