2JBJ
membrane-bound glutamate carboxypeptidase II (GCPII) in complex with 2-PMPA (2-phosphonoMethyl-pentanedioic acid)
Summary for 2JBJ
| Entry DOI | 10.2210/pdb2jbj/pdb |
| Related | 1Z8L 2C6C 2C6G 2C6P 2CIJ 2JBK |
| Descriptor | GLUTAMATE CARBOXYPEPTIDASE 2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total) |
| Functional Keywords | multifunctional enzyme, neurodegenerative disease, glycoprotein, metal-binding, signal-anchor, hydrolase, naaladase, dipeptidase, polymorphism, zinc, psma, antigen, membrane, protease, peptidase, transmembrane, metal- binding, metalloprotease, prostate cancer, carboxypeptidase, alternative splicing |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cell membrane; Single-pass type II membrane protein. Isoform PSMA': Cytoplasm: Q04609 |
| Total number of polymer chains | 1 |
| Total formula weight | 82732.73 |
| Authors | Mesters, J.R.,Henning, K.,Hilgenfeld, R. (deposition date: 2006-12-07, release date: 2006-12-18, Last modification date: 2024-10-16) |
| Primary citation | Mesters, J.R.,Henning, K.,Hilgenfeld, R. Human Glutamate Carboxypeptidase II Inhibition: Structures of Gcpii in Complex with Two Potent Inhibitors, Quisqualate and 2-Pmpa. Acta Crystallogr.,Sect.D, 63:508-, 2007 Cited by PubMed 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 A, 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. PubMed: 17372356DOI: 10.1107/S090744490700902X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.19 Å) |
Structure validation
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