2OOT

A High Resolution Structure of Ligand-free Human Glutamate Carboxypeptidase II

Summary for 2OOT

• Entry DOI: 10.2210/pdb2oot/pdb
• 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, ... (8 entities in total)
• Functional Keywords: metallopeptidase, folate hydrolase, prostate-specific membrane antigen, naaladase, gcpii, hydrolase
• 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: 82547.70

Authors

Barinka, C.,Lubkowski, J. (deposition date: 2007-01-26, release date: 2007-03-20, Last modification date: 2024-11-06)

Primary citation

Barinka, C.,Starkova, J.,Konvalinka, J.,Lubkowski, J.
A high-resolution structure of ligand-free human glutamate carboxypeptidase II.
Acta Crystallogr.,Sect.F, 63:150-153, 2007

PubMed Abstract: Human glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) is an established marker for prostate-cancer diagnosis as well as a candidate therapeutic target for the treatment of diverse pathologies that involve glutamatergic transmission. Structural data on GCPII are thus valuable for the design and optimization of GCPII-specific inhibitors and diagnostic probes. The currently available structure of ligand-free GCPII was refined to a resolution of 3.5 A. This work reports the structure of the protein refined to 1.65 A resolution, with crystallographic values of R = 0.207 and R(free) = 0.228. The new structure extends the resolution appreciably and the new model based on this data shows significant differences when compared with the previously published model.

PubMed: 17329803
DOI: 10.1107/S174430910700379X

Experimental method

X-RAY DIFFRACTION (1.64 Å)