Structure/Function of Na+/K+ Atpase Atp Binding Domain

Gatto, Craig

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Heart, Lung, and Blood Institute (NHLBI)
• Type: Postdoctoral Individual National Research Service Award (F32)
• Project #: 5F32HL009972-02
• Application #: 2901013
• Study Section: Physiology Study Section (PHY)
• Project Start: 1999-04-01
• Budget Start: 1999-04-01
• Budget End: 2000-01-14
• Support Year: 2
• Fiscal Year: 1999

Institution

• Name: Oregon Health and Science University
• Department: Biochemistry
• Type: Schools of Medicine
• DUNS #: 009584210
• City: Portland
• State: OR
• Country: United States
• Zip Code: 97239

Publications

Zhou, A; Huntington, J A; Carrell, R W (1999) Formation of the antithrombin heterodimer in vivo and the onset of thrombosis. Blood 94:3388-96

Gatto, C; Thornewell, S J; Holden, J P et al. (1999) Cys(577) is a conformationally mobile residue in the ATP-binding domain of the Na,K-ATPase alpha-subunit. J Biol Chem 274:24995-5003

Gatto, C; Lutsenko, S; Shin, J M et al. (1999) Stabilization of the H,K-ATPase M5M6 membrane hairpin by K+ ions. Mechanistic significance for p2-type atpases. J Biol Chem 274:13737-40