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Parvalbumin
From Proteopedia
(Difference between revisions)
(New page: Crystal Structure of Parvalbumin 4cpv {{STRUCTURE_4cpv| PDB=4cpv | SIZE=300| SCENE= |right|CAPTION=Parvalbumin 4cpv }}) |
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| - | [[ | + | <StructureSection load='' size='350' side='right' caption='Pike parvalbumin complex with Ca+2 ions (green), ammonium ion (blue), acetyl and formate (PDB entry [[2pvb]])' scene='46/466520/Cv/2' pspeed='8'> |
| - | {{ | + | == Function == |
| + | '''Parvalbumin (PVA)''' is a calcium-binding albumin protein. PVA is involved in calcium signaling<ref>PMID:11867433</ref>. PVA contains 3 domains each containing 2 helices: AB, CD (N-terminal) and EF (C-terminal). '''α-parvalbumin''' differs from '''β-parvalbumin''' in 54 positions. α-parvalbumin is expressed in various tissues while β-parvalbumin is expressed only in preterm placenta<ref>PMID:8354278</ref>. <br /> | ||
| + | See also<br /> | ||
| + | * [[EF hand]] | ||
| + | * [[Parvalbumin carp]]. | ||
| + | |||
| + | == Relevance == | ||
| + | PVA is a major fish allergen<ref>PMID:18221468</ref>. | ||
| + | |||
| + | == Structural highlights == | ||
| + | PVA contains a <scene name='46/466520/Cv/10'>heptacoordinated Ca+2 ion binding to 7 oxygen atoms</scene> in a <scene name='46/466520/Cv/11'>typical EF-hand</scene> coordination<ref>PMID:10548066</ref>. Water molecules are shown as red spheres. <scene name='46/466520/Cv/12'>Calcium ion is coordinated by seven oxygen atoms that form a pentagonal bipyramid </scene>. | ||
| + | *<scene name='46/466520/Cv/13'>Ammonium ion coordination site</scene>. | ||
| + | </StructureSection> | ||
| + | == 3D Structures of Parvalbumin == | ||
| + | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| + | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| + | |||
| + | *parvalbumin | ||
| + | |||
| + | **[[4cpv]], [[5cpv]] – cPVA - carp<br /> | ||
| + | **[[1cdp]] – cPVA Cd-substituted<br /> | ||
| + | **[[1b8c]], [[1b8r]], [[1b9a]], [[1b8l]] – cPVA (mutant)<br /> | ||
| + | **[[1pal]], [[2pal]], [[3pal]], [[4pal]], [[1pvb]], [[1pva]], [[2pvb]] – pPVA – pike<br /> | ||
| + | **[[2pas]], [[3pat]] – pPVA – NMR<br /> | ||
| + | **[[1a75]] – PVA – whiting<br /> | ||
| + | **[[1bu3]] – PVA Ca-binding domain – hake<br /> | ||
| + | **[[5zgm]] – MgPVA SPV-I – ''Mustelus griseus''<br /> | ||
| + | **[[5zh6]] – MgPVA SPV-II<br /> | ||
| + | |||
| + | *α-parvalbumin | ||
| + | |||
| + | **[[1rjv]], [[1rk9]] - hPVA-α - human – NMR<br /> | ||
| + | **[[1rtp]], [[1rwy]] - rPVA-α - rat<br /> | ||
| + | **[[2jww]] - rPVA-α Ca-free – NMR<br /> | ||
| + | **[[1g33]], [[1s3p]], [[1xvj]], [[3f45]] - rPVA-α (mutant)<br /> | ||
| + | **[[5pal]] – PVA-α - shark<br /> | ||
| + | |||
| + | *β-parvalbumin (oncomodulin) | ||
| + | |||
| + | **[[1ttx]] - hPVA-β (mutant) – NMR<br /> | ||
| + | **[[2nln]] - rPVA-β Ca-free – NMR<br /> | ||
| + | **[[1rro]], [[1omd]] - rPVA-β <br /> | ||
| + | **[[3fs7]] - chPVA-β - chicken<br /> | ||
| + | **[[2kqy]] – chPVA-β – NMR<br /> | ||
| + | **[[2kyc]] - chPVA-β <br /> | ||
| + | **[[2kyf]] - chPVA-β (mutant) – NMR<br /> | ||
| + | **[[2mbx]] - PVA-β – cod - NMR<br /> | ||
| + | **[[5xnd]] - PVA-β – mackerel - NMR<br /> | ||
| + | }} | ||
| + | == References == | ||
| + | <references/> | ||
| + | [[Category:Topic Page]] | ||
Current revision
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3D Structures of Parvalbumin
Updated on 05-December-2021
References
- ↑ Cates MS, Teodoro ML, Phillips GN Jr. Molecular mechanisms of calcium and magnesium binding to parvalbumin. Biophys J. 2002 Mar;82(3):1133-46. PMID:11867433 doi:http://dx.doi.org/10.1016/S0006-3495(02)75472-6
- ↑ Fohr UG, Weber BR, Muntener M, Staudenmann W, Hughes GJ, Frutiger S, Banville D, Schafer BW, Heizmann CW. Human alpha and beta parvalbumins. Structure and tissue-specific expression. Eur J Biochem. 1993 Aug 1;215(3):719-27. PMID:8354278
- ↑ Lim DL, Neo KH, Yi FC, Chua KY, Goh DL, Shek LP, Giam YC, Van Bever HP, Lee BW. Parvalbumin--the major tropical fish allergen. Pediatr Allergy Immunol. 2008 Aug;19(5):399-407. doi:, 10.1111/j.1399-3038.2007.00674.x. Epub 2008 Jan 25. PMID:18221468 doi:http://dx.doi.org/10.1111/j.1399-3038.2007.00674.x
- ↑ Declercq JP, Evrard C, Lamzin V, Parello J. Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 A) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic core. Protein Sci. 1999 Oct;8(10):2194-204. PMID:10548066
