Parvalbumin: Difference between revisions

Latest revision as of 12:52, 5 December 2021

Function

Parvalbumin (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].

Relevance

PVA is a major fish allergen^[3].

Structural highlights

PVA contains a in a coordination^[4]. Water molecules are shown as red spheres. .

.

Pike parvalbumin complex with Ca+2 ions (green), ammonium ion (blue), acetyl and formate (PDB entry 2pvb)

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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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Joel L. Sussman

[1] 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

[2] 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

[3] 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

[4] 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

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@@ Line 1: / Line 1: @@
-{{STRUCTURE_4cpv|  PDB=4cpv  | SIZE=300| SCENE=Parvalbumin/Cv/1 |right|CAPTION=Parvalbumin complex with acetate and Ca+2 ions [[4cpv]] }}
+<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]].
-'''Parvalbumin (PVA)''' is a calcium-binding albumin protein.  PVA is involved in calcium signaling.  PVA contains 3 domains: AB, CD (N-terminal) and EF (C-terminal). <br />
+== Relevance ==
-See also [[EF hand]].
+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}}
@@ Line 15: / Line 24: @@
 **[[1pal]], [[2pal]], [[3pal]], [[4pal]], [[1pvb]], [[1pva]], [[2pvb]] – pPVA – pike<br />
 **[[2pas]], [[3pat]] – pPVA – NMR<br />
-**[[1a75]] – PVA – whiting
+**[[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
-**[[5pal]] – PVA-α - shark<br />
+**[[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 />
-**[[1rjv]], [[1rk9]] - hPVA-α - human – NMR
+**[[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 />
-**[[1ttx]] - hPVA-β (mutant) – NMR<br />
 **[[3fs7]] - chPVA-β - chicken<br />
 **[[2kqy]] – chPVA-β – NMR<br />
 **[[2kyc]] - chPVA-β <br />
-**[[2kyf]] - chPVA-β (mutant) – NMR
+**[[2kyf]] - chPVA-β (mutant) – NMR<br />
+**[[2mbx]] - PVA-β – cod - NMR<br />
+**[[5xnd]] - PVA-β – mackerel - NMR<br />
 }}
+== References ==
+<references/>
 [[Category:Topic Page]]