Sandbox bcce03

How is structure related to function in Carp Parvalbumin?

Function: Carp Parvalbumin found in Carp (Cyprinus Carpio) is known to bind calcium ions.

Disease: Currently, Parvalbumin is not known to be directly related to any diseased state.

Relevance: However, the basic structure of Parvalbumin, and its structural calcium binding motif, the EF hand is found in other calcium proteins such as troponin C, involved in skeletal and cardiac muscular contraction, and calmodulin, which is involved in signal transduction

Structural highlights: Parvalbumin is primarily helical, consisting of six alpha helices, labelled, A, B, C, D, E, and F. The CD calcium binding loop binds one calcium ion (in green); the C and D helices encompassing this loop are light and dark green, respectively. The EF calcium binding loop binds one additional calcium ion (in green); the E and F helices, encompassing this loop are yellow and red, respectively. Note the small molecule shown is acetaldehye.

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