Sandbox bcce03

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== Function: == <scene name='59/596444/Carp_parvabumin_4cpv/3'>TextToBeDisplayed</scene>Carp Parvalbumin found in Carp (Cyprinus Carpio) is known to bind calcium ions.==
 
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== Disease: Currently, Parvalbumin is not known to be directly related to any diseased state. ==
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Function: Carp parvalbumin is a calcium binding Protein.
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== 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==
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== 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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Disease: Parvalbumin is not directly related to a diseased state.
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Relevance: The basic structural unit of calcium binding, the EF calcium binding site, is found
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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.
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The EF hand contains the E helix in yellow, the loop, and the F helix in red. The calcium ion is green.
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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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Current revision

How is Structure Related to Function in Carp Parvalbumin?

Carp Parvalbumin 4CPV

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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] ==

  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
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