-
Something wrong with this record ?
Structural basis for the interaction between carbonic anhydrase and 1,2,3,4-tetrahydroisoquinolin-2-ylsulfonamides
P. Mader, J. Brynda, R. Gitto, S. Agnello, P. Pachl, CT. Supuran, A. Chimirri, P. Řezáčová
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
21395315
DOI
10.1021/jm2000213
Knihovny.cz E-resources
- MeSH
- Carbonic Anhydrase Inhibitors chemistry metabolism pharmacology MeSH
- Isoquinolines chemistry metabolism pharmacology MeSH
- Isoenzymes antagonists & inhibitors chemistry metabolism MeSH
- Carbonic Anhydrase II antagonists & inhibitors chemistry metabolism MeSH
- Protein Conformation MeSH
- Crystallography, X-Ray MeSH
- Humans MeSH
- Models, Molecular MeSH
- Substrate Specificity MeSH
- Protein Binding MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Isoquinolinesulfonamides inhibit human carbonic anhydrases (hCAs) and display selectivity toward therapeutically relevant isozymes. The crystal structure of hCA II in complex with 6,7-dimethoxy-1-methyl-1,2,3,4-tetrahydroisoquinolin-2-ylsulfonamide revealed unusual inhibitor binding. Structural analyses allowed for discerning the fine details of the inhibitor binding mode to the active site, thus providing clues for the future design of even more selective inhibitors for druggable isoforms such as the cancer associated hCA IX and neuronal hCA VII.
Dipartimento Farmaco Chimico Università di Messina Messina Italy
Laboratorio di Chimica Bioinorganica Università degli Studi di Firenze Italy
References provided by Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc12027016
- 003
- CZ-PrNML
- 005
- 20160502065439.0
- 007
- ta
- 008
- 120816s2011 xxu f 000 0#eng||
- 009
- AR
- 024 7_
- $a 10.1021/jm2000213 $2 doi
- 035 __
- $a (PubMed)21395315
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a xxu
- 100 1_
- $a Mader, Pavel $7 xx0140528 $u Department of Structural Biology, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic
- 245 10
- $a Structural basis for the interaction between carbonic anhydrase and 1,2,3,4-tetrahydroisoquinolin-2-ylsulfonamides / $c P. Mader, J. Brynda, R. Gitto, S. Agnello, P. Pachl, CT. Supuran, A. Chimirri, P. Řezáčová
- 520 9_
- $a Isoquinolinesulfonamides inhibit human carbonic anhydrases (hCAs) and display selectivity toward therapeutically relevant isozymes. The crystal structure of hCA II in complex with 6,7-dimethoxy-1-methyl-1,2,3,4-tetrahydroisoquinolin-2-ylsulfonamide revealed unusual inhibitor binding. Structural analyses allowed for discerning the fine details of the inhibitor binding mode to the active site, thus providing clues for the future design of even more selective inhibitors for druggable isoforms such as the cancer associated hCA IX and neuronal hCA VII.
- 650 _2
- $a karboanhydrasa II $x antagonisté a inhibitory $x chemie $x metabolismus $7 D024402
- 650 _2
- $a inhibitory karboanhydras $x chemie $x metabolismus $x farmakologie $7 D002257
- 650 _2
- $a krystalografie rentgenová $7 D018360
- 650 _2
- $a lidé $7 D006801
- 650 _2
- $a izoenzymy $x antagonisté a inhibitory $x chemie $x metabolismus $7 D007527
- 650 _2
- $a isochinoliny $x chemie $x metabolismus $x farmakologie $7 D007546
- 650 _2
- $a molekulární modely $7 D008958
- 650 _2
- $a vazba proteinů $7 D011485
- 650 _2
- $a konformace proteinů $7 D011487
- 650 _2
- $a substrátová specifita $7 D013379
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Brynda, Jiří $7 xx0100180 $u Department of Structural Biology, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic; Structural Biology Team, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague, Czech Republic
- 700 1_
- $a Gitto, Rosaria $u Dipartimento Farmaco-Chimico, Università di Messina, Messina, Italy
- 700 1_
- $a Agnello, Stefano $u Dipartimento Farmaco-Chimico, Università di Messina, Messina, Italy $7 gn_A_00002198
- 700 1_
- $a Pachl, Petr $u Department of Structural Biology, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic
- 700 1_
- $a Supuran, Claudiu T $u Laboratorio di Chimica Bioinorganica, Università degli Studi di Firenze, Italy
- 700 1_
- $a Chimirri, Alba $u Dipartimento Farmaco-Chimico, Università di Messina, Messina, Italy
- 700 1_
- $a Řezáčová, Pavlína $7 xx0119409 $u Department of Structural Biology, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic; Structural Biology Team, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague, Czech Republic
- 773 0_
- $w MED00010049 $t Journal of medicinal chemistry $x 1520-4804 $g Roč. 54, č. 7 (2011), s. 2522-2526
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/21395315 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y m $z 0
- 990 __
- $a 20120816 $b ABA008
- 991 __
- $a 20160502065541 $b ABA008
- 999 __
- $a ok $b bmc $g 949058 $s 784362
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2011 $b 54 $c 7 $d 2522-2526 $e 20110311 $i 1520-4804 $m Journal of medicinal chemistry $n J Med Chem $x MED00010049
- LZP __
- $b NLK122 $a Pubmed-20120816/11/02
