Structure-function analysis of the ion channel selectivity filter in human annexin V.
Science
; 262(5132): 427-30, 1993 Oct 15.
Article
em En
| MEDLINE
| ID: mdl-7692599
ABSTRACT
Electrophysiology and structural studies were performed on an annexin V variant containing a mutation of glutamic acid-95 to serine in the center of the pore region. The mutation resulted in a lower single channel conductance for calcium and a strongly increased conductance for sodium and potassium, indicating that glutamic acid-95 is a crucial constituent of the ion selectivity filter. There were only minor differences in the crystal structures of mutant and wild-type annexin V around the mutation site; however, the mutant showed structural differences elsewhere, including the presence of a calcium binding site in domain III unrelated to the mutation. Analysis of the membrane-bound form of annexin V by electron microscopy revealed no differences between the wild type and mutant.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Anexina A5
/
Canais Iônicos
Limite:
Humans
Idioma:
En
Revista:
Science
Ano de publicação:
1993
Tipo de documento:
Article
País de afiliação:
Alemanha