Parvalbumin: Difference between revisions
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<StructureSection load=' | <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 == | == 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 /> | '''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 /> | ||
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== Structural highlights == | == Structural highlights == | ||
PVA contains a <scene name='46/466520/Cv/ | 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> | </StructureSection> | ||
== 3D Structures of Parvalbumin == | == 3D Structures of Parvalbumin == | ||
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**[[1a75]] – PVA – whiting<br /> | **[[1a75]] – PVA – whiting<br /> | ||
**[[1bu3]] – PVA Ca-binding domain – hake<br /> | **[[1bu3]] – PVA Ca-binding domain – hake<br /> | ||
**[[5zgm]] – MgPVA SPV-I – ''Mustelus griseus''<br /> | |||
**[[5zh6]] – MgPVA SPV-II<br /> | |||
*α-parvalbumin | *α-parvalbumin | ||
**[[ | **[[1rjv]], [[1rk9]] - hPVA-α - human – NMR<br /> | ||
**[[1rtp]], [[1rwy]] - rPVA-α - rat<br /> | **[[1rtp]], [[1rwy]] - rPVA-α - rat<br /> | ||
**[[2jww]] - rPVA-α Ca-free – NMR<br /> | **[[2jww]] - rPVA-α Ca-free – NMR<br /> | ||
**[[1g33]], [[1s3p]], [[1xvj]], [[3f45]] - rPVA-α (mutant)<br /> | **[[1g33]], [[1s3p]], [[1xvj]], [[3f45]] - rPVA-α (mutant)<br /> | ||
**[[ | **[[5pal]] – PVA-α - shark<br /> | ||
*β-parvalbumin (oncomodulin) | *β-parvalbumin (oncomodulin) | ||
**[[1ttx]] - hPVA-β (mutant) – NMR<br /> | |||
**[[2nln]] - rPVA-β Ca-free – NMR<br /> | **[[2nln]] - rPVA-β Ca-free – NMR<br /> | ||
**[[1rro]], [[1omd]] - rPVA-β <br /> | **[[1rro]], [[1omd]] - rPVA-β <br /> | ||
**[[3fs7]] - chPVA-β - chicken<br /> | **[[3fs7]] - chPVA-β - chicken<br /> | ||
**[[2kqy]] – chPVA-β – NMR<br /> | **[[2kqy]] – chPVA-β – NMR<br /> | ||
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**[[2kyf]] - chPVA-β (mutant) – NMR<br /> | **[[2kyf]] - chPVA-β (mutant) – NMR<br /> | ||
**[[2mbx]] - PVA-β – cod - NMR<br /> | **[[2mbx]] - PVA-β – cod - NMR<br /> | ||
**[[5xnd]] - PVA-β – mackerel - NMR<br /> | |||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Latest revision as of 12:52, 5 December 2021
FunctionParvalbumin (PVA) is a calcium-binding albumin protein. PVA is involved in calcium signaling[1]. 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[2]. See also RelevancePVA is a major fish allergen[3]. Structural highlightsPVA contains a in a coordination[4]. Water molecules are shown as red spheres. .
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3D Structures of Parvalbumin3D Structures of Parvalbumin
Updated on 05-December-2021
ReferencesReferences
- ↑ 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