1ywh
From Proteopedia
(New page: 200px<br /> <applet load="1ywh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ywh, resolution 2.70Å" /> '''crystal structure o...) |
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| - | [[Image:1ywh.gif|left|200px]]<br /> | + | [[Image:1ywh.gif|left|200px]]<br /><applet load="1ywh" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ywh" size=" | + | |
caption="1ywh, resolution 2.70Å" /> | caption="1ywh, resolution 2.70Å" /> | ||
'''crystal structure of urokinase plasminogen activator receptor'''<br /> | '''crystal structure of urokinase plasminogen activator receptor'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report the crystal structure of a soluble form of human urokinase-type | + | We report the crystal structure of a soluble form of human urokinase-type plasminogen activator receptor (uPAR/CD87), which is expressed at the invasive areas of the tumor-stromal microenvironment in many human cancers. The structure was solved at 2.7 A in association with a competitive peptide inhibitor of the urokinase-type plasminogen activator (uPA)-uPAR interaction. uPAR is composed of three consecutive three-finger domains organized in an almost circular manner, which generates both a deep internal cavity where the peptide binds in a helical conformation, and a large external surface. This knowledge combined with the discovery of a convergent binding motif shared by the antagonist peptide and uPA allowed us to build a model of the human uPA-uPAR complex. This model reveals that the receptor-binding module of uPA engages the uPAR central cavity, thus leaving the external receptor surface accessible for other protein interactions (vitronectin and integrins). By this unique structural assembly, uPAR can orchestrate the fine interplay with the partners that are required to guide uPA-focalized proteolysis on the cell surface and control cell adhesion and migration. |
==About this Structure== | ==About this Structure== | ||
| - | 1YWH 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 NDG, NAG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1YWH 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=NDG:'>NDG</scene>, <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YWH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dano, K.]] | [[Category: Dano, K.]] | ||
| - | [[Category: Du, M | + | [[Category: Du, M H.Le.]] |
[[Category: Gardsvoll, H.]] | [[Category: Gardsvoll, H.]] | ||
[[Category: Gilquin, B.]] | [[Category: Gilquin, B.]] | ||
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[[Category: Menez, A.]] | [[Category: Menez, A.]] | ||
[[Category: Ploug, M.]] | [[Category: Ploug, M.]] | ||
| - | [[Category: Stura, E | + | [[Category: Stura, E A.]] |
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: NDG]] | [[Category: NDG]] | ||
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[[Category: upar]] | [[Category: upar]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:49 2008'' |
Revision as of 14:09, 21 February 2008
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crystal structure of urokinase plasminogen activator receptor
Overview
We report the crystal structure of a soluble form of human urokinase-type plasminogen activator receptor (uPAR/CD87), which is expressed at the invasive areas of the tumor-stromal microenvironment in many human cancers. The structure was solved at 2.7 A in association with a competitive peptide inhibitor of the urokinase-type plasminogen activator (uPA)-uPAR interaction. uPAR is composed of three consecutive three-finger domains organized in an almost circular manner, which generates both a deep internal cavity where the peptide binds in a helical conformation, and a large external surface. This knowledge combined with the discovery of a convergent binding motif shared by the antagonist peptide and uPA allowed us to build a model of the human uPA-uPAR complex. This model reveals that the receptor-binding module of uPA engages the uPAR central cavity, thus leaving the external receptor surface accessible for other protein interactions (vitronectin and integrins). By this unique structural assembly, uPAR can orchestrate the fine interplay with the partners that are required to guide uPA-focalized proteolysis on the cell surface and control cell adhesion and migration.
About this Structure
1YWH is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the human urokinase plasminogen activator receptor bound to an antagonist peptide., Llinas P, Le Du MH, Gardsvoll H, Dano K, Ploug M, Gilquin B, Stura EA, Menez A, EMBO J. 2005 May 4;24(9):1655-63. Epub 2005 Apr 7. PMID:15861141
Page seeded by OCA on Thu Feb 21 16:09:49 2008
Categories: Homo sapiens | Single protein | Dano, K. | Du, M H.Le. | Gardsvoll, H. | Gilquin, B. | Llinas, P. | Menez, A. | Ploug, M. | Stura, E A. | NAG | NDG | SO4 | Protein-peptide complex | Three-finger fold | Upar
