3mfv

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[[Image:3mfv.png|left|200px]]
 
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{{STRUCTURE_3mfv| PDB=3mfv | SCENE= }}
{{STRUCTURE_3mfv| PDB=3mfv | SCENE= }}
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===Crystal structure of human arginase I in complex with 2-aminohomohistidine===
===Crystal structure of human arginase I in complex with 2-aminohomohistidine===
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{{ABSTRACT_PUBMED_20441173}}
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==Disease==
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[[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==
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<ref group="xtra">PMID:020441173</ref><references group="xtra"/>
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<ref group="xtra">PMID:020441173</ref><references group="xtra"/><references/>
[[Category: Arginase]]
[[Category: Arginase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]

Revision as of 22:03, 24 March 2013

Template:STRUCTURE 3mfv

Contents

Crystal structure of human arginase I in complex with 2-aminohomohistidine

Template:ABSTRACT PUBMED 20441173

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

3mfv is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Ilies M, Di Costanzo L, North ML, Scott JA, Christianson DW. 2-aminoimidazole amino acids as inhibitors of the binuclear manganese metalloenzyme human arginase I. J Med Chem. 2010 May 27;53(10):4266-76. PMID:20441173 doi:10.1021/jm100306a
  1. ↑ 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
  2. ↑ 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

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