Journal article
Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family.
- Abstract:
-
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
Actions
Access Document
- Files:
-
-
(Version of record, doc, 10.1MB)
-
(Version of record, pdf, 1.3MB)
-
- Publisher copy:
- 10.1186/1472-6807-12-14
Why is the content I wish to access not available via ORA?
Bibliographic data (the information relating to research outputs) and full-text items (e.g. articles, theses, reports, etc.) arrive in ORA from several different sources. Unfortunately we are not able to make available the full-text for every research output.
Please contact the ORA team (
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
Content may be unavailable for the following four reasons
-
Version unsuitable
-
We have not obtained a suitable full-text for a given research output. See this page for more information.
-
Recently completed
-
Sometimes content is held in ORA but is unavailable for a fixed period of time to comply with the policies and wishes of rights holders.
-
Permissions
-
All content made available in ORA should comply with relevant rights, such as copyright. See this page for more information.
-
Clearance
-
Some thesis volumes scanned as part of the digitisation scheme funded by Dr Leonard Polonsky are currently unavailable due to sensitive material or uncleared third-party copyright content. We are attempting to contact authors whose theses are affected.
Alternative access to the full-text
You may be able to access the full-text directly from the publisher's website using the 'Publisher Copy' link in the 'Links & Downloads' box from a research output's ORA record page. This method may require an institutional or individual subscription to the journal/resource.
Authors
Funding
Canadian Institutes of Health Research
More from this funder
Canadian Foundation for Innovation
More from this funder
Karolinska Institute
More from this funder
GlaxoSmithKline
More from this funder
Genome Canada
More from this funder
Expand funders...
Bibliographic Details
- Publisher:
- BioMed Central Publisher's website
- Journal:
- BMC structural biology Journal website
- Volume:
- 12
- Issue:
- 1
- Pages:
- 14
- Publication date:
- 2012-01-01
- DOI:
- EISSN:
-
1472-6807
- ISSN:
-
1472-6807
- Source identifiers:
-
340011
Item Description
- Language:
- English
- Keywords:
- UUID:
-
uuid:a9c8fa80-f938-49c4-b6ef-8ad449ef84d6
- Local pid:
- pubs:340011
- Deposit date:
- 2012-12-19
Terms of use
- 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.
- Licence:
- CC Attribution (CC BY)
If you are the owner of this record, you can report an update to it here: Report update to this record