Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
The structure of the N-domain of porcine alpha(2) Na,K-ATPase was determined crystallographically to 3.2A resolution by isomorphous heavy-atom replacement using a single mercury derivative. The structure was finally refined against 2.6A resolution synchrotron data. The domain forms a seven-stranded antiparallel beta-sheet with two additional beta-strands forming a hairpin and five alpha-helices. Approximately 75% of the residues were superimposable with residues from the structure of Ca-ATPase N-domain, and a structure-based sequence alignment is presented. The positions of key residues are discussed in relation to the pattern of hydrophobicity, charge and sequence conservation of the molecular surface. The structure of a hexahistidine tag binding to nickel ions is presented.
The crystallographic structure of Na,K-ATPase N-domain at 2.6A resolution.,Hakansson KO J Mol Biol. 2003 Oct 3;332(5):1175-82. PMID:14499619[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hakansson KO. The crystallographic structure of Na,K-ATPase N-domain at 2.6A resolution. J Mol Biol. 2003 Oct 3;332(5):1175-82. PMID:14499619
