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Drug-Target Interaction

Drug

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PubChem ID:3547
Structure:
Synonyms:
(5-ISOQUINOLINESULFONYL)HOMOPIPERAZINE
1-(5-Isoquinolinesulfonyl)homopiperazine
1-(5-Isoquinolinesulphonyl)homopiperazine
1-(5-Isoquinolinylsulfonyl)homopiperazine
1-(5-Isoquinolylsulfonyl)-1,4-diazaperhydroepine
103745-39-7
105628-07-7
105628-07-7(HYDROCHLORIDE)
1H-1,4-Diazepine, hexahydro-1-(5-isoquinolinylsulfonyl)-
1H-1,4-Diazepine, hexahydro-1-(5-isoquinolinylsulfonyl)- (9CI)
1q8w
2esm
2gni
5-(1,4-DIAZEPAN-1-SULFONYL)ISOQUINOLINE
5-(1,4-diazepan-1-ylsulfonyl)isoquinoline
5-(1,4-diazepane-1-sulfonyl)isoquinoline
AC1L1G6K
AC1Q6UWJ
AC1Q6VJ2
AIDS-108016
AIDS108016
AR-1A6371
AT 877
AT-877
AT877
Bio2_000386
Bio2_000866
BiomolKI2_000046
BiomolKI_000038
BRD-K76617868-001-02-2
BRD-K76617868-001-03-0
BRD-K76617868-300-03-6
BRD-K76617868-300-04-4
BSPBio_001111
C14H17N3O2S
CCG-100642
CHEMBL38380
D07941
DB08162
Eril
Fasudil
Fasudil (HA-1077)
Fasudil (INN)
Fasudil hydrochloride
Fasudil [INN]
Fasudilum
Fasudilum [INN-Latin]
FH
HA 1077
HA-1077
HA1077
Hexahydro-1-(5-isoquinolinylsulfonyl)-1H-1,4-diazepine
Hexahydro-1-(5-isoquinolylsulfonyl)-1H-1,4-diazepine
HMS1362G13
HMS1792G13
HMS1990G13
HMS2089F13
HMS3264M10
I06-1557
IDI1_002141
KBio2_000451
KBio2_003019
KBio2_005587
KBio3_000841
KBio3_000842
KBioGR_000451
KBioSS_000451
Kinome_3390
Kinome_3391
KST-1A0465
LS-60220
M77
NCGC00018100-01
NCGC00018100-02
NCGC00018100-03
NCGC00018100-04
NCGC00018100-05
NCGC00018100-06
NCGC00018100-07
NCGC00024299-02
NCGC00024299-04
NCGC00024299-05
SMP2_000083
ST51053125
Tocris-0541
UNII-Q0CH43PGXS
ATC-Codes:

Target

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Uniprot ID:KAPCG_HUMAN
Synonyms:
cAMP-dependent protein kinase catalytic subunit gamma
PKA C-gamma
EC-Numbers:2.7.11.11
Organism:Homo sapiens
Human
PDB IDs:-

Binding Affinities:

Ki: Kd:Ic 50:Ec50/Ic50:
----

References:

16249185
The structure of dimeric ROCK I reveals the mechanism for ligand selectivity.. Marc Jacobs; Koto Hayakawa; Lora Swenson; Steven Bellon; Mark Fleming; Paul Taslimi; John Doran (2006) The Journal of biological chemistry display abstract
ROCK or Rho-associated kinase, a serine/threonine kinase, is an effector of Rho-dependent signaling and is involved in actin-cytoskeleton assembly and cell motility and contraction. The ROCK protein consists of several domains: an N-terminal region, a kinase catalytic domain, a coiled-coil domain containing a RhoA binding site, and a pleckstrin homology domain. The C-terminal region of ROCK binds to and inhibits the kinase catalytic domains, and this inhibition is reversed by binding RhoA, a small GTPase. Here we present the structure of the N-terminal region and the kinase domain. In our structure, two N-terminal regions interact to form a dimerization domain linking two kinase domains together. This spatial arrangement presents the kinase active sites and regulatory sequences on a common face affording the possibility of both kinases simultaneously interacting with a dimeric inhibitory domain or with a dimeric substrate. The kinase domain adopts a catalytically competent conformation; however, no phosphorylation of active site residues is observed in the structure. We also determined the structures of ROCK bound to four different ATP-competitive small molecule inhibitors (Y-27632, fasudil, hydroxyfasudil, and H-1152P). Each of these compounds binds with reduced affinity to cAMP-dependent kinase (PKA), a highly homologous kinase. Subtle differences exist between the ROCK- and PKA-bound conformations of the inhibitors that suggest that interactions with a single amino acid of the active site (Ala215 in ROCK and Thr183 in PKA) determine the relative selectivity of these compounds. Hydroxyfasudil, a metabolite of fasudil, may be selective for ROCK over PKA through a reversed binding orientation.