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Structure paper

TitleStructural locations and functional roles of new subsites S5, S6, and S7 in memapsin 2 (beta-secretase).
Journal, issue, pagesBiochemistry, Vol. 44, Page 105-112, Year 2005
Publish dateOct 4, 2004 (structure data deposition date)
AuthorsTurner III, R.T. / Hong, L. / Koelsch, G. / Ghosh, A.K. / Tang, J.
External linksBiochemistry / PubMed:15628850
MethodsX-ray diffraction
Resolution1.9 - 2 Å
Structure data

PDB-1xn2:
New substrate binding pockets for beta-secretase.
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1xn3:
Crystal structure of Beta-secretase bound to a long inhibitor with additional upstream residues.
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / beta secretase / memapsin2 / BACE / ASP2 / Aspartic protease / Alzheimer's disease / Drug design / HYDROLASE-HYDROLASE INHIBITOR complex

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