- Abstract:
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BACKGROUND: Aspartyl aminopeptidase (DNPEP), with specificity towards an acidic amino acid at the N-terminus, is the only mammalian member among the poorly understood M18 peptidases. DNPEP has implicated roles in protein and peptide metabolism, as well as the renin-angiotensin system in blood pressure regulation. Despite previous enzyme and substrate characterization, structural details of DNPEP regarding ligand recognition and catalytic mechanism remain to be delineated. RESULTS: The crystal...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
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(doc, 10.1MB)
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(pdf, 1.3MB)
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- Publisher copy:
- 10.1186/1472-6807-12-14
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- Publisher:
- BioMed Central Ltd. Publisher's website
- Journal:
- BMC structural biology Journal website
- Volume:
- 12
- Issue:
- 1
- Pages:
- 14
- Publication date:
- 2012-01-01
- DOI:
- EISSN:
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1472-6807
- ISSN:
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1472-6807
- URN:
-
uuid:a9c8fa80-f938-49c4-b6ef-8ad449ef84d6
- Source identifiers:
-
340011
- Local pid:
- pubs:340011
- Copyright holder:
- Chaikuad et al.
- Copyright date:
- 2012
- Notes:
- © 2012 Chaikuad et al.; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Journal article
Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family.
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Canadian Institutes of Health Research
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Canadian Foundation for Innovation
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Genome Canada
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GlaxoSmithKline
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Karolinska Institute
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