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Comment
. 2010 May 4;107(18):8047-8.
doi: 10.1073/pnas.1003436107. Epub 2010 Apr 26.

Yet another "active" pseudokinase, Erb3

Susan S Taylor  1 , Alexandr P Kornev
Affiliations
Comment

Yet another "active" pseudokinase, Erb3

Susan S Taylor et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Erb3-specific residues contribute to a conformation that is different from a typical active kinase. There are two structural motifs that are novel to Erb3, in contrast to an active kinase. One is the 310 helix in the activation segment of the C-lobe (dark red). The other, in the N-lobe, is the truncated αC Helix (teal) and the resulting linker (bright red) that joins it to β strand 3. Phe734, His740, and Asp838 are all residues that are unique to Erb3, and each contributes to this conformation in specific ways. Also shown is how the N-lobe is anchored through the β3–αC loop to the N-terminal linker of a symmetry-related molecule.
See this image and copyright information in PMC

Comment on

References

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