2jbk: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2jbk.gif|left|200px]]<br /> | [[Image:2jbk.gif|left|200px]]<br /><applet load="2jbk" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2jbk" size="450" 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 /> | ||
==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. | |||
==Disease== | ==Disease== | ||
| Line 8: | Line 10: | ||
==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 NAG, ZN, CA, CL and QUS 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] | 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 NAG, ZN, CA, CL and QUS 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2JBK OCA]. | ||
==Reference== | |||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17372356 17372356] | |||
[[Category: Glutamate carboxypeptidase II]] | [[Category: Glutamate carboxypeptidase II]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| Line 37: | Line 42: | ||
[[Category: protease]] | [[Category: protease]] | ||
[[Category: psma]] | [[Category: psma]] | ||
[[Category: signal-anchor]] | [[Category: signal-anchor]] | ||
[[Category: transmembrane]] | [[Category: transmembrane]] | ||
[[Category: zinc]] | [[Category: zinc]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:58:45 2007'' | ||
Revision as of 20:48, 18 December 2007
|
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.
DiseaseDisease
Known diseases associated with this structure: Myocardial infarcation, susceptibility to OMIM:[602855]
About this StructureAbout this Structure
2JBK is a Single protein structure of sequence from Homo sapiens with NAG, ZN, CA, CL and QUS 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
Page seeded by OCA on Tue Dec 18 19:58:45 2007
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- 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