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Title: Crystal structure of N-{N-[N-acetyl-(S)-leucyl]-(S)-leucyl}norleucinal (ALLN), an inhibitor of proteasome

Abstract

The title compound, C20H37N3O4, also known by the acronym ALLN, is a tripeptidic inhibitor of the proteolytic activity of the proteasomes, enzyme complexes implicated in several neurodegenerative diseases and other disorders, including cancer. Thus, the crystal structure of ALLN, solved from synchrotron radiation diffraction data, revealed the molecules in extended conformation of the backbone and engaging all peptide N and O atoms in intermolecular hydrogen bonds forming an infinite antiparallel β-sheet.

Authors:
 [1];  [1];  [2];  [2]
  1. Peptides International, Inc., Louisville, KY (United States)
  2. Argonne National Lab. (ANL), Argonne, IL (United States)
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1225201
Grant/Contract Number:  
AC02-06CH11357; W-31-109-ENG-38
Resource Type:
Accepted Manuscript
Journal Name:
Acta Crystallographica. Section E, Crystallographic Communications
Additional Journal Information:
Journal Volume: 71; Journal Issue: 3; Journal ID: ISSN 2056-9890
Publisher:
International Union of Crystallography
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; crystal structure; proteasome inhibitor; hydrogen bonding; antiparallel β-sheet

Citation Formats

Czerwinski, Andrzej, Basava, Channa, Dauter, Miroslawa, and Dauter, Zbigniew. Crystal structure of N-{N-[N-acetyl-(S)-leucyl]-(S)-leucyl}norleucinal (ALLN), an inhibitor of proteasome. United States: N. p., 2015. Web. doi:10.1107/S2056989015002091.
Czerwinski, Andrzej, Basava, Channa, Dauter, Miroslawa, & Dauter, Zbigniew. Crystal structure of N-{N-[N-acetyl-(S)-leucyl]-(S)-leucyl}norleucinal (ALLN), an inhibitor of proteasome. United States. https://doi.org/10.1107/S2056989015002091
Czerwinski, Andrzej, Basava, Channa, Dauter, Miroslawa, and Dauter, Zbigniew. Sun . "Crystal structure of N-{N-[N-acetyl-(S)-leucyl]-(S)-leucyl}norleucinal (ALLN), an inhibitor of proteasome". United States. https://doi.org/10.1107/S2056989015002091. https://www.osti.gov/servlets/purl/1225201.
@article{osti_1225201,
title = {Crystal structure of N-{N-[N-acetyl-(S)-leucyl]-(S)-leucyl}norleucinal (ALLN), an inhibitor of proteasome},
author = {Czerwinski, Andrzej and Basava, Channa and Dauter, Miroslawa and Dauter, Zbigniew},
abstractNote = {The title compound, C20H37N3O4, also known by the acronym ALLN, is a tripeptidic inhibitor of the proteolytic activity of the proteasomes, enzyme complexes implicated in several neurodegenerative diseases and other disorders, including cancer. Thus, the crystal structure of ALLN, solved from synchrotron radiation diffraction data, revealed the molecules in extended conformation of the backbone and engaging all peptide N and O atoms in intermolecular hydrogen bonds forming an infinite antiparallel β-sheet.},
doi = {10.1107/S2056989015002091},
journal = {Acta Crystallographica. Section E, Crystallographic Communications},
number = 3,
volume = 71,
place = {United States},
year = {Sun Mar 01 00:00:00 EST 2015},
month = {Sun Mar 01 00:00:00 EST 2015}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record

Figures / Tables:

Figure 1 Figure 1: The molecule of ALLN, showing the atom-labelling scheme. Displacement ellipsoids are drawn at the 50% probability level.

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Works referenced in this record:

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Works referencing / citing this record:

Ceramide Induces the Death of Retina Photoreceptors Through Activation of Parthanatos
journal, November 2018

  • Prado Spalm, Facundo H.; Vera, Marcela S.; Dibo, Marcos J.
  • Molecular Neurobiology, Vol. 56, Issue 7
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Figures/Tables have been extracted from DOE-funded journal article accepted manuscripts.