This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2okn
From Proteopedia
m (Protected "2okn" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2okn.png|left|200px]] | ||
| - | |||
{{STRUCTURE_2okn| PDB=2okn | SCENE= }} | {{STRUCTURE_2okn| PDB=2okn | SCENE= }} | ||
| - | |||
===Crystal Strcture of Human Prolidase=== | ===Crystal Strcture of Human Prolidase=== | ||
| + | ==Disease== | ||
| + | [[http://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN]] Defects in PEPD are a cause of prolidase deficiency (PD) [MIM:[http://omim.org/entry/170100 170100]]. Prolidase deficiency is an autosomal recessive disorder associated with iminodipeptiduria. The clinical phenotype includes skin ulcers, mental retardation, recurrent infections, and a characteristic facies. These features, however are incompletely penetrant and highly variable in both age of onset and severity. There is a tight linkage between the polymorphisms of prolidase and the myotonic dystrophy trait.<ref>PMID:2365824</ref><ref>PMID:8198124</ref><ref>PMID:8900231</ref><ref>PMID:12384772</ref> | ||
| + | |||
| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN]] Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen. | ||
==About this Structure== | ==About this Structure== | ||
[[2okn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OKN OCA]. | [[2okn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OKN OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | <references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Xaa-Pro dipeptidase]] | [[Category: Xaa-Pro dipeptidase]] | ||
Revision as of 05:19, 25 March 2013
Contents |
Crystal Strcture of Human Prolidase
Disease
[PEPD_HUMAN] Defects in PEPD are a cause of prolidase deficiency (PD) [MIM:170100]. Prolidase deficiency is an autosomal recessive disorder associated with iminodipeptiduria. The clinical phenotype includes skin ulcers, mental retardation, recurrent infections, and a characteristic facies. These features, however are incompletely penetrant and highly variable in both age of onset and severity. There is a tight linkage between the polymorphisms of prolidase and the myotonic dystrophy trait.[1][2][3][4]
Function
[PEPD_HUMAN] Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.
About this Structure
2okn is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- ↑ Tanoue A, Endo F, Kitano A, Matsuda I. A single nucleotide change in the prolidase gene in fibroblasts from two patients with polypeptide positive prolidase deficiency. Expression of the mutant enzyme in NIH 3T3 cells. J Clin Invest. 1990 Jul;86(1):351-5. PMID:2365824 doi:http://dx.doi.org/10.1172/JCI114708
- ↑ Ledoux P, Scriver C, Hechtman P. Four novel PEPD alleles causing prolidase deficiency. Am J Hum Genet. 1994 Jun;54(6):1014-21. PMID:8198124
- ↑ Ledoux P, Scriver CR, Hechtman P. Expression and molecular analysis of mutations in prolidase deficiency. Am J Hum Genet. 1996 Nov;59(5):1035-9. PMID:8900231
- ↑ Forlino A, Lupi A, Vaghi P, Icaro Cornaglia A, Calligaro A, Campari E, Cetta G. Mutation analysis of five new patients affected by prolidase deficiency: the lack of enzyme activity causes necrosis-like cell death in cultured fibroblasts. Hum Genet. 2002 Oct;111(4-5):314-22. Epub 2002 Aug 14. PMID:12384772 doi:10.1007/s00439-002-0792-5
Categories: Homo sapiens | Xaa-Pro dipeptidase | Behlke, J. | Buessow, K. | Goetz, F. | Heinemann, U. | Mueller, U. | Niesen, F H. | PSF, Protein Structure Factory. | Roske, Y. | Collagen degradation | Dipeptidase | Disease mutation | Enzyme | Hydrolase | Manganese | Metal-binding | Metalloaminopeptidase | Metallocarboxypeptidase | Metalloprotease | Pepd gene | Peptidase d | Phosphorylation | Protease | Protein structure factory | Psf | Structural genomic | Xaa-pro dipeptidase
