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1nnl

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[[Image:1nnl.png|left|200px]]
 
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{{STRUCTURE_1nnl| PDB=1nnl | SCENE= }}
{{STRUCTURE_1nnl| PDB=1nnl | SCENE= }}
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===Crystal structure of Human Phosphoserine Phosphatase===
===Crystal structure of Human Phosphoserine Phosphatase===
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{{ABSTRACT_PUBMED_12777757}}
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{{ABSTRACT_PUBMED_12777757}}
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==Disease==
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[[http://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:[http://omim.org/entry/614023 614023]]. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.<ref>PMID:14673469</ref>
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==Function==
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[[http://www.uniprot.org/uniprot/SERB_HUMAN SERB_HUMAN]] Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates.<ref>PMID:12777757</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:012777757</ref><references group="xtra"/>
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<ref group="xtra">PMID:012777757</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Phosphoserine phosphatase]]
[[Category: Phosphoserine phosphatase]]

Revision as of 17:12, 24 March 2013

Template:STRUCTURE 1nnl

Contents

Crystal structure of Human Phosphoserine Phosphatase

Template:ABSTRACT PUBMED 12777757

Disease

[SERB_HUMAN] Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:614023]. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.[1]

Function

[SERB_HUMAN] Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates.[2]

About this Structure

1nnl is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Peeraer Y, Rabijns A, Verboven C, Collet JF, Van Schaftingen E, De Ranter C. High-resolution structure of human phosphoserine phosphatase in open conformation. Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):971-7. Epub 2003, May 23. PMID:12777757
  1. ↑ Veiga-da-Cunha M, Collet JF, Prieur B, Jaeken J, Peeraer Y, Rabbijns A, Van Schaftingen E. Mutations responsible for 3-phosphoserine phosphatase deficiency. Eur J Hum Genet. 2004 Feb;12(2):163-6. PMID:14673469 doi:10.1038/sj.ejhg.5201083
  2. ↑ Peeraer Y, Rabijns A, Verboven C, Collet JF, Van Schaftingen E, De Ranter C. High-resolution structure of human phosphoserine phosphatase in open conformation. Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):971-7. Epub 2003, May 23. PMID:12777757

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