Tripeptidyl peptidase
From Proteopedia
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| - | [[Image:2d5l.png|left|200px|thumb|Crystal Structure of Tripeptidyl peptidase ([[2d5l]])]] | ||
| - | {{STRUCTURE_3ee6| PDB=3ee6 | SIZE=400| SCENE= |right|CAPTION=Glycosylated tripeptidyl peptidase dimer complex with sulfate, Zn+2 (grey), Ca+2 (green) and Cl- (green) ions, [[3ee6]]}} | ||
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| + | <StructureSection load='3ee6' size='340' side='right' caption='Glycosylated tripeptidyl peptidase I dimer complex with sulfate, Zn+2 (grey), Ca+2 (green) and Cl- (green) ions, [[3ee6]]' scene=''> | ||
| + | == Function == | ||
[[Tripeptidyl peptidase]] (TPP) is an enzyme which cleaves N-terminal tripeptides from polypeptides.<br /> | [[Tripeptidyl peptidase]] (TPP) is an enzyme which cleaves N-terminal tripeptides from polypeptides.<br /> | ||
* '''TPP-I''' functions in lysosomes.<br /> | * '''TPP-I''' functions in lysosomes.<br /> | ||
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* '''TPP-IV''' is a serine exopeptidase which cleaves proline dipeptides from the N-terminus of polypeptides. | * '''TPP-IV''' is a serine exopeptidase which cleaves proline dipeptides from the N-terminus of polypeptides. | ||
| + | == Didease == | ||
| + | TPP-I participates in lysosomal turnover of proteins in pathological conditions associated with cell injury<ref>PMID:11589013</ref>. TPP-II deficiency is linked to severe autoimmunity<ref>PMID:25414442</ref>. TPP-II has central and peripheral roles in metabolism and hence in fat formation<ref>PMID:17932511</ref>. | ||
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| + | == Structural highlights == | ||
| + | TPP-I catalytic triad is the typical Ser-Glu-Asp and the active site contains an octahedrally coordinated Ca+2 ion<ref>PMID:19038966</ref>. | ||
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| + | </StructureSection> | ||
== 3D Structures of Tripeptidyl peptidase == | == 3D Structures of Tripeptidyl peptidase == | ||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
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**[[2z3z]], [[2dcm]] - PgPro-TPP-IV (mutant)+inhibitor<br /> | **[[2z3z]], [[2dcm]] - PgPro-TPP-IV (mutant)+inhibitor<br /> | ||
}} | }} | ||
| - | + | == References == | |
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 10:24, 22 September 2016
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3D Structures of Tripeptidyl peptidase
Updated on 22-September-2016
References
- ↑ Wisniewski KE, Kida E, Walus M, Wujek P, Kaczmarski W, Golabek AA. Tripeptidyl-peptidase I in neuronal ceroid lipofuscinoses and other lysosomal storage disorders. Eur J Paediatr Neurol. 2001;5 Suppl A:73-9. PMID:11589013
- ↑ Stepensky P, Rensing-Ehl A, Gather R, Revel-Vilk S, Fischer U, Nabhani S, Beier F, Brummendorf TH, Fuchs S, Zenke S, Firat E, Pessach VM, Borkhardt A, Rakhmanov M, Keller B, Warnatz K, Eibel H, Niedermann G, Elpeleg O, Ehl S. Early-onset Evans syndrome, immunodeficiency, and premature immunosenescence associated with tripeptidyl-peptidase II deficiency. Blood. 2015 Jan 29;125(5):753-61. doi: 10.1182/blood-2014-08-593202. Epub 2014, Nov 20. PMID:25414442 doi:http://dx.doi.org/10.1182/blood-2014-08-593202
- ↑ McKay RM, McKay JP, Suh JM, Avery L, Graff JM. Tripeptidyl peptidase II promotes fat formation in a conserved fashion. EMBO Rep. 2007 Dec;8(12):1183-9. Epub 2007 Oct 12. PMID:17932511 doi:http://dx.doi.org/10.1038/sj.embor.7401086
- ↑ Pal A, Kraetzner R, Gruene T, Grapp M, Schreiber K, Gronborg M, Urlaub H, Becker S, Asif AR, Gartner J, Sheldrick GM, Steinfeld R. Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis. J Biol Chem. 2009 Feb 6;284(6):3976-84. Epub 2008 Nov 26. PMID:19038966 doi:10.1074/jbc.M806947200
