Sandbox bcce03
From Proteopedia
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| - | == Function: == | ||
| + | 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. | |
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| + | 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. | ||
</StructureSection> | </StructureSection> | ||
Current revision
How is Structure Related to Function in Carp Parvalbumin?
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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
