Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide

被引：84

作者：

Di Fiore, Anna ^{[1
]}

Monti, Simona Maria ^{[1
]}

Hilvo, Mika ^{[2
,3
,4
]}

Parkkila, Seppo ^{[2
,3
,4
]}

Romano, Vincenza ^{[1
]}

Scaloni, Andrea ^{[5
]}

Pedone, Carlo ^{[1
]}

Scozzafava, Andrea ^{[6
]}

Supuran, Claudiu T. ^{[6
]}

De Simone, Giuseppina ^{[1
]}

机构：

[1] CNR, Ist Biostrutture & Bioimmagini, I-80134 Naples, Italy

[2] Univ Tampere, Inst Med Technol, FIN-33101 Tampere, Finland

[3] Univ Tampere, Sch Med, FIN-33101 Tampere, Finland

[4] Univ Tampere, Tampere Univ Hosp, FIN-33101 Tampere, Finland

[5] CNR, ISPAAM, Lab Prote & Spettrometria Massa, I-80147 Naples, Italy

[6] Univ Florence, Chim Bioorgan Lab, I-50019 Florence, Italy

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2009年 / 74卷 / 01期

关键词：

crystal structure; human carbonic anhydrase XIII; inhibitors.protein-inhibitor complex; rational drug design; ISOZYME-II; X-RAY; PROTON-TRANSFER; THERAPEUTIC APPLICATIONS; ANTITUMOR SULFONAMIDE; EXTRACELLULAR DOMAIN; REFINED STRUCTURE; BINDING-SITE; CA-XIII; MEMBRANE;

D O I：

10.1002/prot.22144

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The cytosolic isoform XIII is a recently discovered member of the human carbonic anhydrase (hCA, EC 4.2.1.1) family. It is selectively expressed among other tissues in the reproductive organs, where it may control pH and ion balance regulation, ensuring thus proper fertilization conditions. The authors report here the X-ray crystallographic structure of this isozyme in the unbound state and in complex with a classical sulfonamide inhibitor, namely acetazolamide. A detailed comparison of the obtained structural data with those already reported for other CA isozymes provides novel insights into the catalytic properties of the members of this protein family. On the basis of the inhibitory properties of acetazolamide against various cytosolic/transmembrane isoforms and the structural differences detected within the active site of the various CA isoforms, further prospects for the design of isozyme-specific CA inhibitors are here proposed.

引用

页码：164 / 175

页数：12

共 66 条

[41] STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC-ANHYDRASE-II
NAIR, SK
KREBS, JF
CHRISTIANSON, DW
FIERKE, CA
[J]. BIOCHEMISTRY, 1995, 34 (12) : 3981 - 3989
[42] UNEXPECTED PH-DEPENDENT CONFORMATION OF HIS-64, THE PROTON SHUTTLE OF CARBONIC ANHYDRASE-II
NAIR, SK
CHRISTIANSON, DW
[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1991, 113 (25) : 9455 - 9458
[43] AMORE - AN AUTOMATED PACKAGE FOR MOLECULAR REPLACEMENT
NAVAZA, J
[J]. ACTA CRYSTALLOGRAPHICA SECTION A, 1994, 50 : 157 - 163
[44] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z
Minor, W
[J]. MACROMOLECULAR CRYSTALLOGRAPHY, PT A, 1997, 276 : 307 - 326
[45] PARANAWITHANA SR, 1991, CARBONIC ANHYDRASE, P14
[46] Carbonic anhydrase activators: Activation of isozyme XIII with amino acids and amines
Parkkila, Seppo
Vullo, Daniela
Puccetti, Luca
Parkkila, Anna-Kaisa
Scozzafava, Andrea
Supuran, Claudiu T.
[J]. BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 2006, 16 (15) : 3955 - 3959
[47] Carbonic anhydrases: Current state of the art, therapeutic applications and future prospects
Pastorekova, S
Parkkila, S
Pastorek, J
Supuran, CT
[J]. JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, 2004, 19 (03) : 199 - 229
[48] Three-dimensional structure of a halotolerant algal carbonic anhydrase predicts halotolerance of a mammalian homolog
Premikumar, L
Greenblatt, HM
Bageshwar, UK
Savchenko, T
Gokhman, I
Sussman, JL
Zamir, A
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (21) : 7493 - 7498
[49] Proton transfer pathways in the mutant His-64-Ala of human carbonic anhydrase II
Roy, Arijit
Taraphder, Srabani
[J]. BIOPOLYMERS, 2006, 82 (06) : 623 - 630
[50] Scozzafava A, 2004, EXPERT OPIN THER PAT, V14, P667, DOI 10.1517/eotp.14.5.667.31276

← 1 2 3 4 5 6 7 →