3gn0: Difference between revisions
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{{STRUCTURE_3gn0| PDB=3gn0 | SCENE= }} | {{STRUCTURE_3gn0| PDB=3gn0 | SCENE= }} | ||
===Crystal structure of human arginase I in complex with difluoromethylornithine (DFMO)=== | ===Crystal structure of human arginase I in complex with difluoromethylornithine (DFMO)=== | ||
{{ABSTRACT_PUBMED_21728378}} | |||
==Disease== | |||
[[http://www.uniprot.org/uniprot/ARGI1_HUMAN ARGI1_HUMAN]] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:[http://omim.org/entry/207800 207800]]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.<ref>PMID:1463019</ref><ref>PMID:7649538</ref> | |||
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:021728378</ref><references group="xtra"/> | <ref group="xtra">PMID:021728378</ref><references group="xtra"/><references/> | ||
[[Category: Arginase]] | [[Category: Arginase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 16:22, 24 March 2013
Crystal structure of human arginase I in complex with difluoromethylornithine (DFMO)
Template:ABSTRACT PUBMED 21728378
Disease
[ARGI1_HUMAN] Defects in ARG1 are the cause of argininemia (ARGIN) [MIM:207800]; also known as hyperargininemia. Argininemia is a rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia, progressive spastic quadriplegia.[1][2]
About this Structure
3gn0 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Ilies M, Di Costanzo L, Dowling DP, Thorn KJ, Christianson DW. Binding of alpha,alpha-Disubstituted Amino Acids to Arginase Suggests New Avenues for Inhibitor Design. J Med Chem. 2011 Jul 18. PMID:21728378 doi:10.1021/jm200443b
- ↑ Uchino T, Haraguchi Y, Aparicio JM, Mizutani N, Higashikawa M, Naitoh H, Mori M, Matsuda I. Three novel mutations in the liver-type arginase gene in three unrelated Japanese patients with argininemia. Am J Hum Genet. 1992 Dec;51(6):1406-12. PMID:1463019
- ↑ Uchino T, Snyderman SE, Lambert M, Qureshi IA, Shapira SK, Sansaricq C, Smit LM, Jakobs C, Matsuda I. Molecular basis of phenotypic variation in patients with argininemia. Hum Genet. 1995 Sep;96(3):255-60. PMID:7649538
