From Proteopedia
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| - | == References == | + | == 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 <ref>PMID: 18673581</ref> == |
| | <references/> | | <references/> |
Revision as of 15:34, 6 August 2014
How is Structure Related to Function in Carp Parvalbumin?
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You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
How is structure related to function in Carp Parvalbumin?
Contents
- 1 Function: jmolSetTarget('1');jmolLink('delete $clickGreenLinkEcho; refresh;setL = \"setLoading();\"; javascript @setL; script /wiki/extensions/Proteopedia/spt/wipeFullLoadButton.spt; ~green = \"TextToBeDisplayed\"; isosurface DELETE; scn = load(\"/wiki/scripts/59/596444/Carp_parvabumin_4cpv/3.spt\"); scn = scn.replace(\'# initialize;\', \'# initialize;\nclearSceneScaleCmd = \"clearSceneScale();\"; javascript @clearSceneScaleCmd;\n\'); scn = scn.replace(\'_setSelectionState;\', \'_setSelectionState; message Scene_finished;\'); scn = scn.replace(\'_setState;\', \'_setState; setButtonsStartingState();\'); scn = scn.replace(\'DORESIZE\', \'\'); script inline scn;','TextToBeDisplayed','TextToBeDisplayed');Carp Parvalbumin found in Carp (Cyprinus Carpio) is known to bind calcium ions.
- 2 Disease: Currently, Parvalbumin is not known to be directly related to any diseased state.
- 3 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
- 4 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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Function: Carp Parvalbumin found in Carp (Cyprinus Carpio) is known to bind calcium ions.
Disease: Currently, Parvalbumin is not known to be directly related to any diseased state.
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 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.
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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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 [3] ==
- ↑ 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
- ↑ 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
