4fgu

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'''Unreleased structure'''
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{{STRUCTURE_4fgu| PDB=4fgu | SCENE= }}
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===Crystal structure of prolegumain===
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{{ABSTRACT_PUBMED_23776206}}
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The entry 4fgu is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/LGMN_HUMAN LGMN_HUMAN]] Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system.
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Authors: Dall, E., Brandstetter, H.
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==About this Structure==
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[[4fgu]] 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=4FGU OCA].
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Description: Crystal structure of prolegumain
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==Reference==
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<ref group="xtra">PMID:023776206</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Legumain]]
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[[Category: Brandstetter, H.]]
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[[Category: Dall, E.]]
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[[Category: Aep]]
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[[Category: Antigen processing]]
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[[Category: Asparaginyl endopeptidase]]
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[[Category: Cancer]]
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[[Category: Cysteine protease]]
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[[Category: Hydrolase]]
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[[Category: Lysosomal]]
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[[Category: Mhcii]]
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[[Category: Proenzyme]]
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[[Category: Substrate specificity]]

Revision as of 14:05, 3 July 2013

Template:STRUCTURE 4fgu

Contents

Crystal structure of prolegumain

Template:ABSTRACT PUBMED 23776206

Function

[LGMN_HUMAN] Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system.

About this Structure

4fgu is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Dall E, Brandstetter H. Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation. Proc Natl Acad Sci U S A. 2013 Jun 17. PMID:23776206 doi:10.1073/pnas.1300686110

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