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Titolo:
Three-dimensional structure of the large cytoplasmic H-4-H-5 loop of Na+/K+-ATPase deduced by restraint-based comparative modeling shows only one ATPbinding site
Autore:
Ettrich, R; Melichercik, M; Teisinger, J; Ettrichova, O; Krumscheid, R; Hofbauerova, K; Kvasnicka, P; Schoner, W; Amler, E;
Indirizzi:
Charles Univ, Dept Phys & Macromol Chem, Prague 12840 2, Czech Republic Charles Univ Prague Czech Republic 12840 2 rague 12840 2, Czech Republic Acad Sci Czech Republ, Inst Physiol, CR-14220 Prague 4, Czech Republic Acad Sci Czech Republ Prague Czech Republic 4 0 Prague 4, Czech Republic Comenius Univ, Fac Math & Phys, Bratislava 84248, Slovakia Comenius Univ Bratislava Slovakia 84248 Phys, Bratislava 84248, Slovakia Univ Giessen, Inst Biochem & Endocrinol, D-35392 Giessen, Germany Univ Giessen Giessen Germany D-35392 ndocrinol, D-35392 Giessen, Germany
Titolo Testata:
JOURNAL OF MOLECULAR MODELING
fascicolo: 6, volume: 7, anno: 2001,
pagine: 184 - 192
SICI:
1610-2940(2001)7:6<184:TSOTLC>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLECULAR-DYNAMICS SIMULATION; P-TYPE ATPASE; ESCHERICHIA-COLI; HIGH-AFFINITY; SPATIAL RESTRAINTS; DEHALOGENASE FOLD; PROTEIN; NA,K-ATPASE; DOMAIN; NA+,K+-ATPASE;
Keywords:
sodium potassium adenosine triphosphatase; tertiary structure; adenosine triphosphate binding site; restraint-based homology modeling;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Ettrich, R Charles Univ, Dept Phys & Macromol Chem, Albertov 2030, Prague 12840 2, Czech Republic Charles Univ Albertov 2030 Prague Czech Republic 12840 2 ublic
Citazione:
R. Ettrich et al., "Three-dimensional structure of the large cytoplasmic H-4-H-5 loop of Na+/K+-ATPase deduced by restraint-based comparative modeling shows only one ATPbinding site", J MOL MODEL, 7(6), 2001, pp. 184-192

Abstract

Homology modeling of the complete structure of the large cytoplasmic loop between the fourth and fifth transmembrane segments (H-4-H-5 loop) of the alpha subunit of Na+/K+-ATPase is reported. The deduced amino acid sequence shows high sequence identity and homology to the Ca2+-ATPase (32.8% identity and 53.3% similarity in our alignment), whose tertiary structure has beensolved recently at 2.6-Angstrom resolution by X-ray crystallography. This high homology allowed the construction of a model structure using the MODELLER program. Refinement was achieved through interactive visual and algorithmic analysis and minimization with the TRIPOS force field included in the SYBYL/MAXIMIN2 module. The docking of ATP as a substrate into the active site of the model was explored with the AUTODOCK program followed by molecular mechanics optimization of the most interesting complexes. Thus, the docking of ATP into the resulting model of the H-4-H-5 loop gave evidence for the existence of one ATP binding site only. We were able to specify Cys(549),Phe(548), Glu(505), Lys(501), Gln(482), Lys(480), Ser(477), Phe(475) and Glu(446) as parts of the ATP binding site with Lys(501) located in the depthof the positively charged binding pocket.

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Documento generato il 23/01/20 alle ore 06:26:10