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The structural stability of the large cytoplasmic domain (H4-H5loop) of mouse a1subunit of Na+/K+ATPase (L354–I777), the number and the location of its binding sites for2¢-3¢-O-(trinitrophenyl) adenosine 5¢-triphosphate (TNP-ATP) andp-nitrophenylphosphate (pNPP) were investi-gated. C- and N-terminal shortening revealed that neitherpart of the phosphorylation (P)-domain are necessary forTNP-ATP binding. There is no indication of a second ATPsite on the P-domain of the isolated loop, even thoughothers reported previously of its existence by TNP-N3ADPaffinity labeling of the full enzyme. ...
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site
