Sandbox bcce03

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(→Structure Function Relationships in Carp Parvalbumin)
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==How is Structure Related to Function in Carp Parvalbumin?)==
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==How is Structure Related to Function in Carp Parvalbumin?==
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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<StructureSection load='1stp' size='340' side='right' caption='Carp Parvalbumin 4CPV' scene='59/596444/Carp_parvabumin_4cpv/4'>
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This is a default text for your page '''Sandbox bcce03'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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How is structure related to function in Carp Parvalbumin?
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== Function ==
 
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== Disease ==
 
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== Relevance ==
 
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== Structural highlights ==
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Function: Carp parvalbumin is a calcium binding Protein.
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> 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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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.
</StructureSection>
</StructureSection>
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== References ==
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== References: Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5-A resolution.
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Kumar, V.D., Lee, L., Edwards, B.F.
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(1990) Biochemistry 29: 1404-1412. Pubmed 2334704
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<ref>PMID: 18673581</ref> ==
<references/>
<references/>

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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