4awb: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4awb|  PDB=4awb  |  SCENE=  }}
===Crystal structure of active legumain in complex with AAN-CMK===
{{ABSTRACT_PUBMED_23776206}}


The entry 4awb is ON HOLD  until Paper Publication
==Function==
[[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.


Authors: Dall, E., Brandstetter, H.
==About this Structure==
[[4awb]] is a 4 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=4AWB OCA].  


Description: Crystal structure of active legumain in complex with AAN-CMK
==Reference==
<ref group="xtra">PMID:023776206</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Legumain]]
[[Category: Brandstetter, H.]]
[[Category: Dall, E.]]
[[Category: Aep]]
[[Category: Antigen processing]]
[[Category: Cancer]]
[[Category: Cysteine protease]]
[[Category: Hydrolase]]
[[Category: Hydrolase-inhibitor complex]]
[[Category: Lysosomal]]
[[Category: Mhcii]]
[[Category: Substrate specificity]]

Revision as of 09:51, 30 June 2013

Template:STRUCTURE 4awb

Crystal structure of active legumain in complex with AAN-CMK

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

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

Reference

  1. 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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