Conformational changes induced in the endoplasmic reticulum luminal domain of calnexin by Mg-ATP and Ca2

The type I membrane protein calnexin functions as a molecular chaperone for secretory glycoproteins in the endoplasmic reticulum with ATP and Ca2+ as two of the cofactors involved in substrate binding. Protease protection experiments with intact canine rough microsomes showed that amino acid residue...

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Veröffentlicht in:	The Journal of biological chemistry 1995-07, Vol.270 (30), p.18051-18059
Hauptverfasser:	Ou, W J, Bergeron, J J, Li, Y, Kang, C Y, Thomas, D Y
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism AIDS/HIV Amino Acid Sequence Animals Baculoviridae - genetics Calcium - metabolism Calcium-Binding Proteins - chemistry Calcium-Binding Proteins - isolation & purification Calcium-Binding Proteins - metabolism Calnexin Cell Line Disulfides - metabolism Dogs Endopeptidases - metabolism Endoplasmic Reticulum - metabolism HIV Envelope Protein gp120 - metabolism HIV-1 - metabolism Humans Molecular Sequence Data Protein Binding Protein Conformation Sequence Homology, Amino Acid Spodoptera
Online-Zugang:	Volltext
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