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Titolo:
SEQUENCE OF A MENKES-TYPE CU-TRANSPORTING ATPASE FROM RAT C6 GLIOMA-CELLS - COMPARISON OF THE RAT PROTEIN WITH OTHER MAMMALIAN CU-TRANSPORTING ATPASES
Autore:
QIAN YC; TIFFANYCASTIGLIONI E; HARRIS ED;
Indirizzi:
TEXAS A&M UNIV,DEPT BIOCHEM & BIOPHYS COLLEGE STN TX 77843 TEXAS A&M UNIV,DEPT BIOCHEM & BIOPHYS COLLEGE STN TX 77843 TEXAS A&M UNIV,DEPT VET ANAT & PUBL HLTH COLLEGE STN TX 77843
Titolo Testata:
Molecular and cellular biochemistry
fascicolo: 1-2, volume: 181, anno: 1998,
pagine: 49 - 61
SICI:
0300-8177(1998)181:1-2<49:SOAMCA>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
WILSON-DISEASE GENE; P-TYPE ATPASES; SECONDARY STRUCTURE; CANDIDATE GENE; NEURAL NETWORKS; MURINE HOMOLOG; COPPER; MOUSE; MUTATIONS; PREDICTION;
Keywords:
MENKES GENE; MENKES TRANSCRIPT; CU-ATPASE; HEAVY METAL BINDING DOMAIN; RAT BRAIN ATPASE; COPPER HOMEOSTASIS; C6 RAT GLIOMA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
35
Recensione:
Indirizzi per estratti:
Citazione:
Y.C. Qian et al., "SEQUENCE OF A MENKES-TYPE CU-TRANSPORTING ATPASE FROM RAT C6 GLIOMA-CELLS - COMPARISON OF THE RAT PROTEIN WITH OTHER MAMMALIAN CU-TRANSPORTING ATPASES", Molecular and cellular biochemistry, 181(1-2), 1998, pp. 49-61

Abstract

Rat Atp7a occupied a single open reading frame (27-4502) which coded for a protein of 1492 residues. Rat Atp7a was 98% and 95% identical topublished sequences for the mouse and Chinese hamster, respectively, and 94% homologous to human ATP7A. Compared to ATP7A, the rat transcript coded for an additional alanine (A446) in the heavy metal binding (Hmb) domain and showed a 34 bp gap in the 3'UTR. Based on published sequence data, hydropathic profiles for rat, mouse, Chinese hamster, andhuman Cu-ATPases were practically identical with the exception of 8 additional amino acid residues between the 4th and 5th Hmb sites in thehuman. As deduced from amino acid sequence data, Hmb was predicted tohave regions with helical and beta structures. All four species had five of the six metal binding sites centered within hydrophobic regions. The comparative analyses suggested that the Hmb region of the molecule could experience numerous amino acid substitutions with no apparentdisruption to the ATPase transport function whereas variations to theATPase domain would be more critical.

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Documento generato il 29/11/20 alle ore 16:17:09