From Proteopedia
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| - | == Disease: == Currently, Parvalbumin is not known to be directly related to any diseased state. == | + | == Disease: == |
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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== | + | == Relevance:== |
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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. == | + | == Structural highlights:== |
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Revision as of 15:57, 6 August 2014
How is Structure Related to Function in Carp Parvalbumin?
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Function:
Disease:
Relevance:
Structural highlights:
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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
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- ↑ 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
