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[[Image:2jbk.gif|left|200px]]<br /><applet load="2jbk" size=" | [[Image:2jbk.gif|left|200px]]<br /><applet load="2jbk" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2jbk, resolution 2.99Å" /> | caption="2jbk, resolution 2.99Å" /> | ||
'''MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II (GCPII) IN COMPLEX WITH QUISQUALIC ACID (QUISQUALATE, ALPHA-AMINO-3,5-DIOXO-1,2,4-OXADIAZOLIDINE-2-PROPANOIC ACID)'''<br /> | '''MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II (GCPII) IN COMPLEX WITH QUISQUALIC ACID (QUISQUALATE, ALPHA-AMINO-3,5-DIOXO-1,2,4-OXADIAZOLIDINE-2-PROPANOIC ACID)'''<br /> | ||
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==Overview== | ==Overview== | ||
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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
2JBK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG: | 2JBK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=QUS:'>QUS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] Known structural/functional Sites: <scene name='pdbsite=AC1:Zn Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:Zn Binding Site For Chain A'>AC2</scene>, <scene name='pdbsite=AC3:Ca Binding Site For Chain A'>AC3</scene>, <scene name='pdbsite=AC4:Cl Binding Site For Chain A'>AC4</scene>, <scene name='pdbsite=AC5:Nag Binding Site For Chain A'>AC5</scene>, <scene name='pdbsite=AC6:Nag Binding Site For Chain A'>AC6</scene>, <scene name='pdbsite=AC7:Nag Binding Site For Chain A'>AC7</scene>, <scene name='pdbsite=AC8:Nag Binding Site For Chain A'>AC8</scene>, <scene name='pdbsite=AC9:Nag Binding Site For Chain A'>AC9</scene>, <scene name='pdbsite=BC1:Nag Binding Site For Chain A'>BC1</scene>, <scene name='pdbsite=BC2:Nag Binding Site For Chain A'>BC2</scene>, <scene name='pdbsite=BC3:Nag Binding Site For Chain A'>BC3</scene>, <scene name='pdbsite=BC5:Nag Binding Site For Chain A'>BC5</scene>, <scene name='pdbsite=BC6:Nag Binding Site For Chain A'>BC6</scene>, <scene name='pdbsite=BC7:Bma Binding Site For Chain A'>BC7</scene> and <scene name='pdbsite=BC9:Qus Binding Site For Chain A'>BC9</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JBK OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:12:30 2008'' | ||
Revision as of 13:12, 23 January 2008
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MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II (GCPII) IN COMPLEX WITH QUISQUALIC ACID (QUISQUALATE, ALPHA-AMINO-3,5-DIOXO-1,2,4-OXADIAZOLIDINE-2-PROPANOIC ACID)
OverviewOverview
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.
About this StructureAbout this Structure
2JBK is a Single protein structure of sequence from Homo sapiens with , , , and as ligands. Active as Glutamate carboxypeptidase II, with EC number 3.4.17.21 Known structural/functional Sites: , , , , , , , , , , , , , , and . Full crystallographic information is available from OCA.
ReferenceReference
Human glutamate carboxypeptidase II inhibition: structures of GCPII in complex with two potent inhibitors, quisqualate and 2-PMPA., Mesters JR, Henning K, Hilgenfeld R, Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):508-13. Epub 2007, Mar 16. PMID:17372356
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Pages with broken file links
- Glutamate carboxypeptidase II
- Homo sapiens
- Single protein
- Henning, K.
- Hilgenfeld, R.
- Mesters, J.R.
- CA
- CL
- NAG
- QUS
- ZN
- Antigen
- Carboxypeptidase
- Dipeptidase
- Glycoprotein
- Hydrolase
- Membrane
- Metal- binding
- Metal-binding
- Metalloprotease
- Multifunctional enzyme
- Naaladase
- Neurodegenerative disease
- Peptidase
- Polymorphism
- Prostate cancer
- Protease
- Psma
- Signal-anchor
- Transmembrane
- Zinc