The π-helix formation between Asp369 and Thr375 as a key factor in E1-E2 conformational change of Na+/K+-ATPase

Title:

The π-helix formation between Asp369 and Thr375 as a key factor in E1-E2 conformational change of Na+/K+-ATPase

Creator:

Tejral, G., Koláčná, L., Wolfgang Schöner, and Evžen Amler

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:a82d89fd-32a3-40c7-b930-354b33342614
uuid:a82d89fd-32a3-40c7-b930-354b33342614

Subject:

Biochemie. Molekulární biologie. Biofyzika, biochemie, počítačové modelování, struktura molekul, biochemistry, computer modeling, molecular structure, molecular dynamics simulations, Na+/K+-ATPase, E1/E2 conformation, 2, and 577

Type:

article, články, model:article, and TEXT

Description:

Molecular modeling of the H4-H5-loop of the α2 isoform of Na+/K+-ATPase in the E1 and E2 conformations revealed that twisting of the nucleotide (N) domain toward the phosphorylation (P) domain is connected with the formation of a short π-helix between Asp369 and Thr375. This conformational change close to the hinge region between the N-domain and the P-domain could be an important event leading to a bending of the N-domain by 64.7° and to a shortening of the distance between the ATP binding site and the phosphorylation site (Asp369) by 1.22 nm from 3.22 nm to 2.00 nm. It is hypothesized that this shortening mechanism is involved in the Na+-dependent formation of the Asp369 phospho-intermediate as part of the overall Na+/K+-ATPase activity., G. Tejral ... [et al.]., and Obsahuje seznam literatury

Language:

English

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Source:

Physiological research | 2009 Volume:58 | Number:4

Harvested from:

CDK

Metadata only:

false