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Open Access Highly Accessed Research article

Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family

Apirat Chaikuad1, Ewa S Pilka1, Antonio De Riso2, Frank von Delft1, Kathryn L Kavanagh1, Catherine Vénien-Bryan2, Udo Oppermann13 and Wyatt W Yue1*

Author Affiliations

1 Structural Genomics Consortium, Old Road Research Campus Building, Oxford OX3 7DQ, UK

2 Laboratory of Molecular Biophysics, Department of Biochemistry, Oxford, OX1 3QU, UK

3 Botnar Research Centre, Oxford Biomedical Research Unit, Oxford, OX3 7LD, UK

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BMC Structural Biology 2012, 12:14  doi:10.1186/1472-6807-12-14

Published: 21 June 2012

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Additional file:

Figure S1. Domain swapping inthe hDNPEP dimer. Figure S2. Tetrahedron complexes of available bacterial M18 structures. Figure S3. Architecture of the wide and narrow channels. Figure S4. hDNPEP P1 substrate pocket. Figure S5. Substrate peptide modelling into hDNPEP [34-37].

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