Serpin: Difference between revisions

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<StructureSection load='2xn6' size='350' side='right' caption='Structure of cleaved human serpin A7.  Residues 32-380 (cyan), residues 381-415 (salmon) complex with thyroxine-fluoresein, ethylene glycol and Ca+2 ion (green) (PDB entry [[2xn6]])' scene='51/517379/Cv/1'>
<StructureSection load='2xn6' size='350' side='right' caption='Structure of cleaved human serpin A7.  Residues 32-380 (grey), residues 381-415 (green) complex with thyroxine-fluoresein (PDB entry [[2xn6]])' scene=''>
== Function ==
== Function ==
'''Serpin or serine protease inhibitor''' (Ser) are protease inhibitors.<br />
'''Serpin or serine protease inhibitor''' (Ser) are protease inhibitors.<br />
Line 20: Line 19:
== Disease ==
== Disease ==
Mutation in Ser A7 causes partial thyroxine-binding globulin deficiency<ref>PMID:24356794</ref>.  Ser B3 may contribute to tumor cell resistance to anti-neoplastic drugs<ref>PMID:25332258</ref>.  Ser A3 promotes growth of endometrial cancer cells <ref>PMID:24817931</ref>.
Mutation in Ser A7 causes partial thyroxine-binding globulin deficiency<ref>PMID:24356794</ref>.  Ser B3 may contribute to tumor cell resistance to anti-neoplastic drugs<ref>PMID:25332258</ref>.  Ser A3 promotes growth of endometrial cancer cells <ref>PMID:24817931</ref>.
</StructureSection>
 
==Structural highlights ==
Ser A7 - a thyrosine-binding globulin - <scene name='51/517379/Cv/3'>binding site contains thyroxin derivative</scene><ref>PMID:21325280</ref>. Water molecules are shown as red spheres.


==3D structures of serpin==
==3D structures of serpin==
[[Serpin 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*Serpin
 
**[[1mtp]], [[1sng]] – Ser – ''Thermobifida fusca''
 
*Serpin A1 see [[Alpha-1-antitrypsin]]
 
*Serpin A3 (α 1-antichymotrypsin)
 
**[[2ach]], [[1as4]], [[3caa]] – hSer-A3<br />
**[[4caa]], [[1qmn]], [[3dlw]] – hSer-A3 (mutant)<br />
**[[1yxa]] – mSer-A3N - mouse<br />
 
*Serpin A5
 
**[[2ol2]] – hSer-A5<br />
**[[3dy0]] – hSer-A5 + heparin
 
*Serpin A6 see [[Corticosteroid-binding globulin]]
 
*Serpin A7
 
**[[2riv]] – hSer-A7<br />
**[[2riw]] – hSer-A7 + thyroxine<br />
**[[2xn3]] – hSer-A7 + mefenamic acid<br />
**[[2xn5]] – hSer-A7 + furosemide<br />
**[[2xn6]], [[2xn7]] – hSer-A7 + thyroxine-fluoresein
 
*Serpin A8
 
**[[2jp8]] – hSer-A8 – NMR<br />
**[[2wxw]] – hSer-A8<br />
**[[2x0b]] – hSer-A8 + renin<br />
**[[2wxx]], [[2wxy]], [[2wy0]] – Ser-A8 – mouse<br />
**[[2wxz]], [[2wy1]] – rSer-A8
 
*Serpin A10
 
**[[3h5c]], [[3f1s]] – hSer-A10 + vitamin K-dependent protein Z
 
*Serpin A12
 
**[[4if8]] – hSer-A12<br />
 
*Serpin B1 (leukocyte elastase inhibitor)
 
**[[1hle]] – Ser-B1 – horse <br />
**[[4ga7]] – hSer-B1 (mutant) <br />
 
*Serpin B3
 
**[[2zv6]] – hSer-B3
 
*Serpin B5 (Maspin)
 
**[[1xqg]], [[1wz9]], [[1xu8]] - hSer-B5<br />
**[[1xqj]] – hSer-B5 (mutant) <br />
 
*Serpin C1 see [[Antithrombin]]
 
*Ser crmA (ice inhibitor)
 
**[[1c8o]], [[1f0c]] – cvSer-crmA (mutant) – cowpox virus<br />
 
*Serpin E1 see [[Plasminogen activator inhibitor]]
 
*Serpin E2
 
**[[4dy0]] – hSer-E2 + heparin
 
*Serpin I1 (Neuroserpin)
 
**[[3fgq]], [[2f02]], [[3f5n]] – hSer-I1<br />
**[[1jjo]] – mSer-I1<br />
 
*Serpin K
 
**[[1sek]] – ThSer-K – Tobacco hornworm
 
*Serpin 1
 
**[[1k9o]] – ThSer-1 (mutant) + trypsin II<br />
**[[3le2]] – Ser-1 – ''Arabidopsis thaliana''
 
*Serpin 2
 
**[[1m93]] – cvSer-2 <br />
**[[3nda]] – Ser-2 – Sheep tick<br />
**[[3pzf]] – mmSer-2 – malaria mosquito<br />
**[[4ro9]], [[4roa]], [[4rob]], [[4rsq]] – mmSer-2 (mutant)<br />
 
*Ser 4 (Serine protease inhibitor 4)
 
**[[4p0f]], [[4p0o]] – Ser-4 – ''Drosophila melanogaster''<br />


}}
== References ==
== References ==
<references/>  
<references/>  
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 14:45, 4 February 2020

Function

Serpin or serine protease inhibitor (Ser) are protease inhibitors.

Disease

Mutation in Ser A7 causes partial thyroxine-binding globulin deficiency[5]. Ser B3 may contribute to tumor cell resistance to anti-neoplastic drugs[6]. Ser A3 promotes growth of endometrial cancer cells [7].

Structural highlights

Ser A7 - a thyrosine-binding globulin - [8]. Water molecules are shown as red spheres.

3D structures of serpin

Serpin 3D structures


Structure of cleaved human serpin A7. Residues 32-380 (cyan), residues 381-415 (salmon) complex with thyroxine-fluoresein, ethylene glycol and Ca+2 ion (green) (PDB entry 2xn6)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ El Ouaamari A, Dirice E, Gedeon N, Hu J, Zhou JY, Shirakawa J, Hou L, Goodman J, Karampelias C, Qiang G, Boucher J, Martinez R, Gritsenko MA, De Jesus DF, Kahraman S, Bhatt S, Smith RD, Beer HD, Jungtrakoon P, Gong Y, Goldfine AB, Liew CW, Doria A, Andersson O, Qian WJ, Remold-O'Donnell E, Kulkarni RN. SerpinB1 Promotes Pancreatic beta Cell Proliferation. Cell Metab. 2016 Jan 12;23(1):194-205. doi: 10.1016/j.cmet.2015.12.001. Epub 2015, Dec 15. PMID:26701651 doi:http://dx.doi.org/10.1016/j.cmet.2015.12.001
  2. ↑ Quarta S, Vidalino L, Turato C, Ruvoletto M, Calabrese F, Valente M, Cannito S, Fassina G, Parola M, Gatta A, Pontisso P. SERPINB3 induces epithelial-mesenchymal transition. J Pathol. 2010 Jul;221(3):343-56. doi: 10.1002/path.2708. PMID:20527027 doi:http://dx.doi.org/10.1002/path.2708
  3. ↑ Maass N, Hojo T, Ueding M, Luttges J, Kloppel G, Jonat W, Nagasaki K. Expression of the tumor suppressor gene Maspin in human pancreatic cancers. Clin Cancer Res. 2001 Apr;7(4):812-7. PMID:11309327
  4. ↑ Zhou Q, Snipas S, Orth K, Muzio M, Dixit VM, Salvesen GS. Target protease specificity of the viral serpin CrmA. Analysis of five caspases. J Biol Chem. 1997 Mar 21;272(12):7797-800. PMID:9065443
  5. ↑ Sklate RT, Olcese MC, Maccallini GC, Sarmiento RG, Targovnik HM, Rivolta CM. Novel mutation p.A64D in the Serpina7 gene as a cause of partial thyroxine-binding globulin deficiency associated with increases affinity in transthyretin by a known p.A109T mutation in the TTR gene. Horm Metab Res. 2014 Feb;46(2):100-8. doi: 10.1055/s-0033-1358741. Epub 2013 Dec , 19. PMID:24356794 doi:http://dx.doi.org/10.1055/s-0033-1358741
  6. ↑ Pontisso P. Role of SERPINB3 in hepatocellular carcinoma. Ann Hepatol. 2014 Nov-Dec;13(6):722-7. PMID:25332258
  7. ↑ Yang GD, Yang XM, Lu H, Ren Y, Ma MZ, Zhu LY, Wang JH, Song WW, Zhang WM, Zhang R, Zhang ZG. SERPINA3 promotes endometrial cancer cells growth by regulating G2/M cell cycle checkpoint and apoptosis. Int J Clin Exp Pathol. 2014 Mar 15;7(4):1348-58. eCollection 2014. PMID:24817931
  8. ↑ Qi X, Loiseau F, Chan WL, Yan Y, Wei Z, Milroy LG, Myers RM, Ley SV, Read RJ, Carrell RW, Zhou A. Allosteric modulation of hormone release from thyroxine and corticosteroid binding-globulins. J Biol Chem. 2011 Feb 16. PMID:21325280 doi:10.1074/jbc.M110.171082

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Michal Harel, Alexander Berchansky
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