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The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Structure of the Protease Domain of Memapsin 2 (β-Secretase) Complexed with Inhibitor

Hong, Lin, Koelsch, Gerald, Lin, Xinli, Wu, Shili, Terzyan, Simon, Ghosh, Arun K., Zhang, Xuenjun C., Tang, Jordan·2000·Science
DOI 10.1126/science.290.5489.150
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Abstract

Memapsin 2 (β-secretase) is a membrane-associated aspartic protease involved in the production of β-amyloid peptide in Alzheimer's disease and is a major target for drug design. We determined the crystal structure of the protease domain of human memapsin 2 complexed to an eight-residue inhibitor at 1.9 angstrom resolution. The active site of memapsin 2 is more open and less hydrophobic than that of other human aspartic proteases. The subsite locations from S 4 to S 2 ′ are well defined. A kink of the inhibitor chain at P 2 ′ and the change of chain direction of P 3 ′ and P 4 ′ may be mimicked to provide inhibitor selectivity.

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Metadata

Authors
Hong, L., Koelsch, G., Lin, X., Wu, S., Terzyan, S., Ghosh, A. K., Zhang, X. C., & Tang, J.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2000-10-06
Volume
290
Issue
5489
Pages
150-153
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.290.5489.150
OpenAlex
W1854324009
Cited by
711
References
1
FWCI
18.14
Type
journal article
Language
en
Open access
closed

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