This title appears in the Scientific Report :
2013
Please use the identifier:
http://hdl.handle.net/2128/5642 in citations.
Please use the identifier: http://dx.doi.org/10.1371/journal.pone.0070095 in citations.
Structural and functional characterization of the recombinant death domain from death-associated protein kinase.
Structural and functional characterization of the recombinant death domain from death-associated protein kinase.
Death-associated protein kinase (DAPk) is a calcium/calmodulin-regulated Ser/Thr-protein kinase that functions at an important point of integration for cell death signaling pathways. DAPk has a structurally unique multi-domain architecture, including a C-terminally positioned death domain (DD) that...
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Personal Name(s): | Dioletis, Evangelos |
---|---|
Dingley, Andrew / Driscoll, Paul C (Corresponding author) | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | PLoS one, 8 (2013) 7, S. e70095 |
Imprint: |
Lawrence, Kan.
PLoS
2013
|
PubMed ID: |
23922916 |
DOI: |
10.1371/journal.pone.0070095 |
Document Type: |
Journal Article |
Research Program: |
Structural Biology |
Link: |
Get full text OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1371/journal.pone.0070095 in citations.
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520 | |a Death-associated protein kinase (DAPk) is a calcium/calmodulin-regulated Ser/Thr-protein kinase that functions at an important point of integration for cell death signaling pathways. DAPk has a structurally unique multi-domain architecture, including a C-terminally positioned death domain (DD) that is a positive regulator of DAPk activity. In this study, recombinant DAPk-DD was observed to aggregate readily and could not be prepared in sufficient yield for structural analysis. However, DAPk-DD could be obtained as a soluble protein in the form of a translational fusion protein with the B1 domain of streptococcal protein G. In contrast to other DDs that adopt the canonical six amphipathic α-helices arranged in a compact fold, the DAPk-DD was found to possess surprisingly low regular secondary structure content and an absence of a stable globular fold, as determined by circular dichroism (CD), NMR spectroscopy and a temperature-dependent fluorescence assay. Furthermore, we measured the in vitro interaction between extracellular-regulated kinase-2 (ERK2) and various recombinant DAPk-DD constructs. Despite the low level of structural order, the recombinant DAPk-DD retained the ability to interact with ERK2 in a 1∶1 ratio with a K d in the low micromolar range. Only the full-length DAPk-DD could bind ERK2, indicating that the apparent 'D-motif' located in the putative sixth helix of DAPk-DD is not sufficient for ERK2 recognition. CD analysis revealed that binding of DAPk-DD to ERK2 is not accompanied by a significant change in secondary structure. Taken together our data argue that the DAPk-DD, when expressed in isolation, does not adopt a classical DD fold, yet in this state retains the capacity to interact with at least one of its binding partners. The lack of a stable globular structure for the DAPk-DD may reflect either that its folding would be supported by interactions absent in our experimental set-up, or a limitation in the structural bioinformatics assignment of the three-dimensional structure. | ||
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