PMID- 25630103
OWN - NLM
STAT- MEDLINE
DCOM- 20150303
LR  - 20190806
IS  - 0301-1208 (Print)
IS  - 0301-1208 (Linking)
VI  - 51
IP  - 5
DP  - 2014 Oct
TI  - In silico analysis of the structure and interaction of COP1 protein of 
      Arabidopsis thaliana.
PG  - 343-9
AB  - Previous studies have shown that COP1 (constitutive photomorphogenic 1) protein 
      of Arabidopsis thaliana plays a crucial role in different aspects of 
      photomorphogenesis. Interaction of COP1 with SPA1 (suppressor of phytochrome A) 
      and other regulatory proteins actively affect light regulatory gene expression in 
      diverse directions. Though several studies have explained the function of COP1 
      protein, method of its interaction with SPA1 and cryptochromes are still not 
      explained in detail. In this study, in silico analysis was followed to predict 
      the tertiary structure, active site residues, functionally important regions and 
      regular expressions of COP1 protein. Its ease of its interaction with SPA1 and 
      seven other regulatory proteins, namely bZIP transcription factor 56 (HY5), 
      transcription factor HY5-like (HYH), serine/threonine-protein phosphatase 7 
      (AtPP7), protein long hypocotyl in FAR-RED 1 (HFR1), OBP3-responsive protein 1 
      (OBP3), transcription factor MYC2 (MYC2/ZBF1) and Z-box binding factor 2 protein 
      (GBF1/ZBF2) was measured using protein-protein docking. Interaction with MYC2 was 
      found to be stronger than with others with a global energy value of -22.46. It 
      was also found that COP1 shared three regions of regular expression with SPA1, 
      the last expression also being present in MYC2/ZBF1 and OBP3. Taken together, the 
      insight into structural and functional properties of COP1 protein presented in 
      this study would be helpful in determining the role of COP1 in unknown mechanisms 
      of photomorphogenesis.
FAU - Karumuri, Sudha
AU  - Karumuri S
FAU - Bandopadhyay, Rajib
AU  - Bandopadhyay R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - India
TA  - Indian J Biochem Biophys
JT  - Indian journal of biochemistry & biophysics
JID - 0310774
RN  - 0 (Arabidopsis Proteins)
RN  - EC 2.3.2.27 (AT2G32950 protein, Arabidopsis)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Arabidopsis Proteins/*chemistry/*ultrastructure
MH  - Binding Sites
MH  - Computer Simulation
MH  - Enzyme Activation
MH  - *Models, Chemical
MH  - Molecular Docking Simulation/*methods
MH  - Molecular Sequence Data
MH  - Protein Binding
MH  - Protein Conformation
MH  - Protein Interaction Mapping/*methods
MH  - Structure-Activity Relationship
MH  - Substrate Specificity
MH  - Ubiquitin-Protein Ligases/*chemistry/*ultrastructure
EDAT- 2015/01/30 06:00
MHDA- 2015/03/04 06:00
CRDT- 2015/01/30 06:00
PHST- 2015/01/30 06:00 [entrez]
PHST- 2015/01/30 06:00 [pubmed]
PHST- 2015/03/04 06:00 [medline]
PST - ppublish
SO  - Indian J Biochem Biophys. 2014 Oct;51(5):343-9.