260
Views
0
CrossRef citations to date
0
Altmetric
Erratum

Erratum

Page 957 | Published online: 01 Jul 2009

Figures & data

Figure 2. Putative JAK2 structure, based on homology with other tyrosine kinases such as fibroblast growth factor, where the crystal structure has been solved. This ribbon diagram displays the active kinase JH1 domain in blue (left) and the pseudokinase JH2 domain in green (right). The activation loop of JH1 on the left side of the diagram is shown twice, in two possible conformations: active (phosphorylated – red) and inactive (non-phosphorylated – navy blue). The JH1 kinase site is shown in orange, and the adenosine triphosphate (ATP) binding site in yellow. Homologous activation loop and kinase domains (non-functional) are shown on JH2 as well. Site of interaction of JH2 and the activation domain of JH1 is shown encircled, along with the location of Val617. Adapted from Kaushansky [114] (Blood 2005) and the American Society of Hematology, with permission, and from Lindauer [86].

Figure 2. Putative JAK2 structure, based on homology with other tyrosine kinases such as fibroblast growth factor, where the crystal structure has been solved. This ribbon diagram displays the active kinase JH1 domain in blue (left) and the pseudokinase JH2 domain in green (right). The activation loop of JH1 on the left side of the diagram is shown twice, in two possible conformations: active (phosphorylated – red) and inactive (non-phosphorylated – navy blue). The JH1 kinase site is shown in orange, and the adenosine triphosphate (ATP) binding site in yellow. Homologous activation loop and kinase domains (non-functional) are shown on JH2 as well. Site of interaction of JH2 and the activation domain of JH1 is shown encircled, along with the location of Val617. Adapted from Kaushansky [114] (Blood 2005) and the American Society of Hematology, with permission, and from Lindauer [86].

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.