Theoretical investigations on the interactions of glucokinase regulatory protein with fructose phosphates
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- 作者：Baoping Ling ; baopingling@mail.qfnu.edu.cn" class="auth_mail" title="E-mail the corresponding author ; Xueyuan Yan ; Min Sun ; Siwei Bi ; siweibi@126.com" class="auth_mail" title="E-mail the corresponding author
- 关键词：GK ; glucokinase ; GKRP ; glucokinase regulatory protein ; F1P ; fructose 1-phosphate ; F6P ; fructose 6-phosphate ; SIS ; sugar isomerase ; PDB ; Protein Data Bank ; MD ; molecular dynamics ; ED analysis ; essential dynamics analysis ; PCA ; principle component analysis ; NVT ; constant volume ; NPT ; constant pressure ; SPC ; simple point charge ; PME ; particle-mesh Ewald ; RMSD ; root mean square deviation ; RMSF ; root mean square fluctuation ; RMSIP ; root mean square inner product ; MM-PBSA ; molecular mechanics Poisson
- 刊名：Computational Biology and Chemistry
- 出版年：2016
- 出版时间：February 2016
- 年：2016
- 卷：60
- 期：Complete
- 页码：21-31
- 全文大小：6198 K
文摘
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F1P and F6P can bind to the same active site with different binding mode.
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Ligands affect the conformational spaces and motions of GKRP.
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Electrostatic interaction provides a major driving force for the ligand binding.
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F6P makes loop2 of GKRP more protruding and strengthens its contacts with GK.
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The residues 179-184 play a critical role in the binding of phosphate group.