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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...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1186/1472-6807-12-14

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Role:
Author
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Canadian Institutes of Health Research More from this funder
Canadian Foundation for Innovation More from this funder
Genome Canada More from this funder
GlaxoSmithKline More from this funder
Karolinska Institute More from this funder
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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:
1472-6807
ISSN:
1472-6807
URN:
uuid:a9c8fa80-f938-49c4-b6ef-8ad449ef84d6
Source identifiers:
340011
Local pid:
pubs:340011

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