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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

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

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
More from this funder
Name:
Knut and Alice Wallenberg Foundation
More from this funder
Name:
Swedish Foundation for Strategic Research
Publisher:
BioMed Central
Journal:
BMC structural biology More from this journal
Volume:
12
Issue:
1
Pages:
14
Publication date:
2012-01-01
DOI:
EISSN:
1472-6807
ISSN:
1472-6807

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