Azurin: Difference between revisions
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<StructureSection load=' | <StructureSection load='1joi' size='350' side='right' caption='Structure of azurin containing Cu+2 ion (PDB code [[1joi]]).' scene='59/593967/Cv/1'> | ||
== Function == | == Function == | ||
'''Azurin''' (AZ) is a blue copper protein. AZ mediates electron transfer and contains type I copper center. | '''Azurin''' (AZ) is a blue copper protein. AZ mediates electron transfer and contains type I copper center.<br /> | ||
For details see [[Intramolecular Electron Transfer in Azurin]]. | |||
== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
= | <scene name='59/593967/Cv/3'>AZ active Cu binding site is shown here</scene>. <ref>PMID:8109977</ref> | ||
==3D structures of azurin== | |||
[[Azurin 3D structures]] | |||
</StructureSection> | |||
Latest revision as of 12:08, 31 March 2019
FunctionAzurin (AZ) is a blue copper protein. AZ mediates electron transfer and contains type I copper center. For details see Intramolecular Electron Transfer in Azurin. RelevanceAZ was found to be a novel anticancer agent. Following the entry of the P. aeruginosa bacteria into human melanoma and breast cancer cells, the AZ complexes with the tumor suppressor p53. The complex stabilizes p53 and activates the apoptosis of the cancer cells. Structural highlights. [1] 3D structures of azurin
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ReferencesReferences
- ↑ Zhu DW, Dahms T, Willis K, Szabo AG, Lee X. Crystallization and preliminary crystallographic studies of the crystals of the azurin Pseudomonas fluorescens. Arch Biochem Biophys. 1994 Feb 1;308(2):469-70. PMID:8109977 doi:http://dx.doi.org/10.1006/abbi.1994.1066