Limits...
The first crystal structure of cyclic GMP-dependent protein kinase I β dimerization/docking domain reveals molecular details of isoform-specific anchoring

View Article: PubMed Central - HTML

No MeSH data available.


Structures of the Dimerization/Docking domains.
© Copyright Policy
Related In: Results  -  Collection


getmorefigures.php?uid=PMC3313374&req=5

Figure 1: Structures of the Dimerization/Docking domains.

Mentions: It is increasingly evident that the fidelity of signal transduction is dependent on the ability of proteins to assemble into pathway specific multiprotein complexes. We also showed that the surrogate domain of the closely related cAMP-dependent protein kinase (PKA) forms an X-type helical bundle (Figure 1), providing a completely different docking surface for binding PKA specific anchoring proteins [1]. The coiled-coil is also a highly important model system for studying fundamental principles in protein folding, stability and specificity.


The first crystal structure of cyclic GMP-dependent protein kinase I β dimerization/docking domain reveals molecular details of isoform-specific anchoring
Structures of the Dimerization/Docking domains.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3313374&req=5

Figure 1: Structures of the Dimerization/Docking domains.
Mentions: It is increasingly evident that the fidelity of signal transduction is dependent on the ability of proteins to assemble into pathway specific multiprotein complexes. We also showed that the surrogate domain of the closely related cAMP-dependent protein kinase (PKA) forms an X-type helical bundle (Figure 1), providing a completely different docking surface for binding PKA specific anchoring proteins [1]. The coiled-coil is also a highly important model system for studying fundamental principles in protein folding, stability and specificity.

View Article: PubMed Central - HTML

No MeSH data available.