Structure, Dynamics and Folding of an Immunoglobulin-like Domain of Actin Binding Protein Palladin

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Issue Date
2017-04
Authors
Vattepu, Ravi
Beck, Moriah R.
Advisor
Citation

Ravi Vattepu and Moriah R Beck Structure, Dynamics and Folding of an Immunoglobulin-like Domain of Actin Binding Protein Palladin FASEB J April 2017 31:762.11

Abstract

While members of the immunoglobulin (Ig) share a very conserved folding pattern, this family is also the most diverse in terms of function and sequence. The conserved ®–sandwich fold of Ig domains provides a stable scaffold to display a variety of binding site sequences on its surface, however it has been suggested that small variations in the fold may add additional flexibility to fulfill specific functions. Among the few known intracellular proteins containing Ig-domains, the muscle-related family is the most common and includes cell adhesion molecules like titin and telokin. Palladin is a recently identified protein from a novel family of actin binding protein that includes myopalladin and myotilin.

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