3u0v

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[[Image:3u0v.jpg|left|200px]]
 
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{{STRUCTURE_3u0v| PDB=3u0v | SCENE= }}
{{STRUCTURE_3u0v| PDB=3u0v | SCENE= }}
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===Crystal Structure Analysis of human LYPLAL1===
===Crystal Structure Analysis of human LYPLAL1===
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{{ABSTRACT_PUBMED_22052940}}
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==Function==
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[[http://www.uniprot.org/uniprot/LYPL1_HUMAN LYPL1_HUMAN]] Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site.<ref>PMID:22052940</ref>
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{{ABSTRACT_PUBMED_22052940}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:022052940</ref><references group="xtra"/>
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<ref group="xtra">PMID:022052940</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Burger, M.]]
[[Category: Burger, M.]]

Revision as of 12:40, 3 July 2013

Template:STRUCTURE 3u0v

Contents

Crystal Structure Analysis of human LYPLAL1

Template:ABSTRACT PUBMED 22052940

Function

[LYPL1_HUMAN] Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site.[1]

About this Structure

3u0v is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Burger M, Zimmermann TJ, Kondoh Y, Stege P, Watanabe N, Osada H, Waldmann H, Vetter IR. Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity in spite of close relationship to acyl protein thioesterases. J Lipid Res. 2011 Nov 3. PMID:22052940 doi:10.1194/jlr.M019851
  1. ↑ Burger M, Zimmermann TJ, Kondoh Y, Stege P, Watanabe N, Osada H, Waldmann H, Vetter IR. Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity in spite of close relationship to acyl protein thioesterases. J Lipid Res. 2011 Nov 3. PMID:22052940 doi:10.1194/jlr.M019851

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OCA

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