In:
Annals of the New York Academy of Sciences, Wiley, Vol. 986, No. 1 ( 2003-04), p. 175-182
Abstract:
A bstract : Gastric H,K‐ATPase has, in the absence of ATP and added ions, a preference for the E 2 conformation. Mutations in the cation‐binding pocket often result in a preference for the E 1 ‐conformation. This can be paralleled by the occurrence of K + ‐ independent ATPase activity. These two phenomena could be separated by combined mutagenesis of several residues in and around the cation‐binding pocket. Models of the three‐dimensional structure of H,K‐ATPase visualize the relationship between the E 1 /E 2 preference and the structure.
Type of Medium:
Online Resource
ISSN:
0077-8923
,
1749-6632
DOI:
10.1111/nyas.2003.986.issue-1
DOI:
10.1111/j.1749-6632.2003.tb07157.x
Language:
English
Publisher:
Wiley
Publication Date:
2003
detail.hit.zdb_id:
2834079-6
detail.hit.zdb_id:
211003-9
detail.hit.zdb_id:
2071584-5
SSG:
11
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