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An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases.

Abstract:

The analysis reported here describes detailed structural studies of endothiapepsin (the aspartic proteinase from Endothia parasitica), with and without bound inhibitors, and human pepsin 3b. Comparison of multiple crystal structures of members of the aspartic proteinase family has revealed small but significant differences in domain orientation in different crystal forms. In this paper, it is shown that these differences in domain orientation do not necessarily correlate with the presence or ...

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Publication status:
Published

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Publisher copy:
10.1107/s0907444912004817

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
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Journal:
Acta crystallographica. Section D, Biological crystallography
Volume:
68
Issue:
Pt 5
Pages:
541-552
Publication date:
2012-05-05
DOI:
EISSN:
1399-0047
ISSN:
0907-4449
URN:
uuid:3a8c34fc-c199-488b-91eb-ce1f441f2eef
Source identifiers:
325220
Local pid:
pubs:325220

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