1y8e
From Proteopedia
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|PDB= 1y8e |SIZE=350|CAPTION= <scene name='initialview01'>1y8e</scene>, resolution 2.2Å | |PDB= 1y8e |SIZE=350|CAPTION= <scene name='initialview01'>1y8e</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SVR:8,8'-[CARBONYLBIS[IMINO-3,1-PHENYLENECARBONYLIMINO(4-METHYL-3,1-PHENYLENE)CARBONYLIMINO]]BIS-1,3,5-NAPHTHALENETRISULFONIC ACID'>SVR</scene> | + | |LIGAND= <scene name='pdbligand=SVR:8,8'-[CARBONYLBIS[IMINO-3,1-PHENYLENECARBONYLIMINO(4-METHYL-3,1-PHENYLENE)CARBONYLIMINO]]BIS-1,3,5-NAPHTHALENETRISULFONIC+ACID'>SVR</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1g44|1G44]], [[1rid|1RID]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y8e OCA], [http://www.ebi.ac.uk/pdbsum/1y8e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y8e RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Muthuvel, S K.]] | [[Category: Muthuvel, S K.]] | ||
[[Category: Smith, S A.]] | [[Category: Smith, S A.]] | ||
| - | [[Category: SVR]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:00:06 2008'' |
Revision as of 22:00, 30 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1G44, 1RID
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
VCP:Suramin Complex
Overview
Suramin is a competitive inhibitor of heparin binding to many proteins, including viral envelope proteins, protein tyrosine phosphatases, and fibroblast growth factors (FGFs). It has been clinically evaluated as a potential therapeutic in treatment of cancers caused by unregulated angiogenesis, triggered by FGFs. Although it has shown clinical promise in treatment of several cancers, suramin has many undesirable side effects. There is currently no experimental structure that reveals the molecular interactions responsible for suramin inhibition of heparin binding, which could be of potential use in structure-assisted design of improved analogues of suramin. We report the structure of suramin, in complex with the heparin-binding site of vaccinia virus complement control protein (VCP), which interacts with heparin in a geometrically similar manner to many FGFs. The larger than anticipated flexibility of suramin manifested in this structure, and other details of VCP-suramin interactions, might provide useful structural information for interpreting interactions of suramin with many proteins.
About this Structure
1Y8E is a Single protein structure of sequence from Vaccinia virus. Full crystallographic information is available from OCA.
Reference
Structural basis for antagonism by suramin of heparin binding to vaccinia complement protein., Ganesh VK, Muthuvel SK, Smith SA, Kotwal GJ, Murthy KH, Biochemistry. 2005 Aug 16;44(32):10757-65. PMID:16086578
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