Computational Chemistry of Protein Kinase A and Its Inhibitor Balanol

被引：0

作者：

Jin Haixiao ^{[1
]}

Yan Xiaojun ^{[1
]}

Zhu Peng ^{[1
]}

机构：

[1] Ningbo Univ, Key Lab Marine Biotechnol, Ningbo 315211, Zhejiang, Peoples R China

来源：

PROGRESS IN CHEMISTRY | 2010年 / 22卷 / 05期

关键词：

protein kinase A (PKA); balanol; molecular dynamics simulation; dock; QM/MM; CATALYTIC SUBUNIT; PHOSPHORYL-TRANSFER; CRYSTAL-STRUCTURE; REGULATORY SUBUNIT; ACTIVE-SITE; LIGAND DOCKING; CAMP; PKA; MECHANISM; BINDING;

D O I：

暂无

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Protein kinases regulate the signal transduction pathways in cell by phosphorylating the protein kinase substrate, and they are important targets in drug design. Protein kinase A (PKA) is the first kinase that was obtained X-ray structure of its catalytic domain, and is regarded as prototype for protein kinase superfamily. The progress in computational chemistry study of protein kinase A has been reviewed, including the molecular dynamics simulation study of PKA holoenzyme and its C subunit and R subunit in aqueous solution, phosphoryl transfer mechanism, the binding free energy predicting and flexible docking of C subunit with its inhibitor balanol. Various computational approaches are applied to this system, including molecular dynamics simulation, dock, homology modeling, QM/MM.

引用

页码：993 / 1001

页数：9

共 55 条

[1] Serine-53 at the tip of the glycine-rich loop of cAMP-dependent protein kinase: Role in catalysis, P-site specificity, and interaction with inhibitors
Aimes, RT
Hemmer, W
Taylor, SS
[J]. BIOCHEMISTRY, 2000, 39 (28) : 8325 - 8332
[2] Balanol analogues probe specificity determinants and the conformational malleability of the cyclic 3′,5′-adenosine monophosphate-dependent protein kinase catalytic subunit
Akamine, P
Madhusudan
Brunton, LL
Ou, HD
Canaves, JM
Xuong, NH
Taylor, SS
[J]. BIOCHEMISTRY, 2004, 43 (01) : 85 - 96
[3] Identification of the protein kinase A regulatory RIα-catalytic subunit interface by amide H/2H exchange and protein docking
Anand, GS
Law, D
Mandell, JG
Snead, AN
Tsigelny, I
Taylor, SS
Ten Eyck, LF
Komives, EA
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (23) : 13264 - 13269
[4] Density functional study of the enzymatic reaction catalyzed by a cyclin-dependent kinase
Cavalli, A
De Vivo, M
Recanatini, M
[J]. CHEMICAL COMMUNICATIONS, 2003, (11) : 1308 - 1309
[5] Representing receptor flexibility in ligand docking through relevant normal modes
Cavasotto, CN
Kovacs, JA
Abagyan, RA
[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (26) : 9632 - 9640
[6] Phosphorylation and activation of cAMP-dependent protein kinase by phosphoinositide-dependent protein kinase
Cheng, XD
Ma, YL
Moore, M
Hemmings, BA
Taylor, SS
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (17) : 9849 - 9854
[7] How does activation loop phosphorylation modulate catalytic activity in the cAMP-dependent protein kinase: A theoretical study
Cheng, YH
Zhang, YK
McCammon, JA
[J]. PROTEIN SCIENCE, 2006, 15 (04) : 672 - 683
[8] How does the cAMP-dependent protein kinase catalyze the phosphorylation reaction: An ab initio QM/MM study
Cheng, YH
Zhang, YK
McCammon, JA
[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (05) : 1553 - 1562
[9] RAS And PKA pathways in cancer: new insight from transcriptional analysis
Chiaradonna, Ferdinando
Balestrieri, Chiara
Gaglio, Daniela
Vanoni, Marco
[J]. FRONTIERS IN BIOSCIENCE-LANDMARK, 2008, 13 : 5257 - 5278
[10] Insights into the phosphoryl-transfer mechanism of cAMP-dependent protein kinase from quantum chemical calculations and molecular dynamics simulations
Díaz, N
Field, MJ
[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2004, 126 (02) : 529 - 542

← 1 2 3 4 5 6 →