Parvalbumin carp
How is Structure Related to Function in Carp Parvalbumin?How is Structure Related to Function in Carp Parvalbumin?
Function: Carp parvalbumin is a calcium binding Protein. Disease: Parvalbumin is not directly related to a diseased state. Relevance: The basic structural unit of calcium binding, the EF calcium binding site, is found in other proteins such as troponin, involved in muscle contraction, and calmodulin, involved in signal transduction and many other processes. Structural highlights: The protein contains eight alpha helices labelled, A, B, C, D, E, and F. The EF hand contains the E helix in yellow, the loop, and the F helix in red. The calcium ion is green. The CD hand contains the C helix in light green, the loop, and the D hand in dark green. The calcium ion is green. The A and B helices are dark blue and teal, respectively, and do not bind calcium. The remaining small molecule is acetaldehyde.
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== References: Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5-A resolution. Kumar, V.D., Lee, L., Edwards, B.F. (1990) Biochemistry 29: 1404-1412. Pubmed 2334704 [1] ==
- ↑ Hodis E, Prilusky J, Martz E, Silman I, Moult J, Sussman JL. Proteopedia - a scientific 'wiki' bridging the rift between three-dimensional structure and function of biomacromolecules. Genome Biol. 2008;9(8):R121. Epub 2008 Aug 3. PMID:18673581 doi:http://dx.doi.org/10.1186/gb-2008-9-8-r121