This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Sandbox bcce03
From Proteopedia
(Difference between revisions)
| (2 intermediate revisions not shown.) | |||
| Line 4: | Line 4: | ||
| - | == 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. | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| + | 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?
| |||||||||||
== 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
