Sandbox bcce03
From Proteopedia
(Difference between revisions)
| Line 11: | Line 11: | ||
== 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: 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== | ||
| - | == 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 EF calcium binding loop binds one additional calcium ion (in green). == | + | == 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. == |
Revision as of 15:15, 6 August 2014
How is Structure Related to Function in Carp Parvalbumin?
| |||||||||||
References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
