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PDBsum entry 1p2a
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Contents |
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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The structure of cyclin dependent kinase 2 (ckd2) with a trisubstituted naphthostyril inhibitor
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Structure:
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Cell division protein kinase 2. Chain: a. Synonym: p33 protein kinase. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: cdk2. Expressed in: unidentified baculovirus. Expression_system_taxid: 10469
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Resolution:
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2.50Å
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R-factor:
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0.206
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R-free:
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0.280
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Authors:
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J.-J.Liu,A.Dermatakis,C.M.Lukacs,F.Konzelmann,Y.Chen,U.Kammlott, W.Depinto,H.Yang,X.Yin,Y.Chen,A.Schutt,M.E.Simcox,K.-C.Luk
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Key ref:
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J.J.Liu
et al.
(2003).
3,5,6-Trisubstituted naphthostyrils as CDK2 inhibitors.
Bioorg Med Chem Lett,
13,
2465-2468.
PubMed id:
DOI:
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Date:
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15-Apr-03
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Release date:
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15-Jul-03
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PROCHECK
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Headers
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References
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P24941
(CDK2_HUMAN) -
Cyclin-dependent kinase 2 from Homo sapiens
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Seq:
Struc:
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298 a.a.
271 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.2.7.11.22
- cyclin-dependent kinase.
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Reaction:
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1.
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L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
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2.
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L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
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L-seryl-[protein]
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+
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ATP
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=
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O-phospho-L-seryl-[protein]
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+
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ADP
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+
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H(+)
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L-threonyl-[protein]
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+
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ATP
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=
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O-phospho-L-threonyl-[protein]
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+
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ADP
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Bioorg Med Chem Lett
13:2465-2468
(2003)
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PubMed id:
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3,5,6-Trisubstituted naphthostyrils as CDK2 inhibitors.
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J.J.Liu,
A.Dermatakis,
C.Lukacs,
F.Konzelmann,
Y.Chen,
U.Kammlott,
W.Depinto,
H.Yang,
X.Yin,
Y.Chen,
A.Schutt,
M.E.Simcox,
K.C.Luk.
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ABSTRACT
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A novel class of 3,5,6-trisubstituted naphthostyril analogues was designed and
synthesized to study the structure-activity relationship for inhibition of
cyclin-dependent kinase 2 (CDK2). These compounds, particularly molecules with
side-chain modifications providing additional hydrogen bonding capability, were
demonstrated to be potent CDK2 inhibitors with cellular activities consistent
with CDK2 inhibition. These molecules inhibited tumor cell proliferation and
G1-S and G2-M cell-cycle progression in vitro. The X-ray crystal structure of a
2-aminoethyleneamine derivative bound to CDK2, refined to 2.5A resolution, is
presented.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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K.Engels,
C.Beyer,
M.L.Suárez Fernández,
F.Bender,
M.Gassel,
G.Unden,
R.J.Marhöfer,
J.C.Mottram,
and
P.M.Selzer
(2010).
Inhibition of Eimeria tenella CDK-related kinase 2: From target identification to lead compounds.
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ChemMedChem,
5,
1259-1271.
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K.Fujimura,
and
Y.Sasabuchi
(2010).
The role of fluorine atoms in a fluorinated prostaglandin agonist.
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ChemMedChem,
5,
1254-1257.
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J.Sridhar,
N.Akula,
and
N.Pattabiraman
(2006).
Selectivity and potency of cyclin-dependent kinase inhibitors.
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AAPS J,
8,
E204-E221.
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H.J.Cristau,
P.P.Cellier,
J.F.Spindler,
and
M.Taillefer
(2004).
Highly efficient and mild copper-catalyzed N- and C-arylations with aryl bromides and iodides.
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Chemistry,
10,
5607-5622.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
