Abstract
Human glutamate carboxypeptidase II (GCPII) occurs in the central nervous system as well as in human prostate (where it is called prostate-specific membrane antigen; PSMA). Inhibitors of the enzyme have been shown to provide neuroprotection, but may also be useful for the detection, imaging and treatment of prostate cancer. Crystal structures were determined of the extracellular part of GCPII (amino-acid residues 44-750) in complex with two potent inhibitors, quisqualate and 2-PMPA (the strongest GCPII inhibitor to date), at resolutions of 3.0 and 2.2 Å, respectively. In addition, models were constructed for binding of the inhibitors willardiine, homoibotenate, l-2-amino-4-phosphonobutanoic acid and l-serine-O-sulfate to the S1′ site of the enzyme. The common denominator for high-affinity binding to the S1′ site is the formation of two strong salt bridges.
| Original language | English |
|---|---|
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 63 |
| Issue number | 4 |
| Pages (from-to) | 508-513 |
| Number of pages | 6 |
| ISSN | 0907-4449 |
| DOIs | |
| Publication status | Published - 16.03.2007 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Research Areas and Centers
- Academic Focus: Center for Infection and Inflammation Research (ZIEL)
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