1cnu: Difference between revisions
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[[Image:1cnu.gif|left|200px]] | [[Image:1cnu.gif|left|200px]] | ||
'''PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA''' | {{Structure | ||
|PDB= 1cnu |SIZE=350|CAPTION= <scene name='initialview01'>1cnu</scene>, resolution 2.25Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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'''PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CNU is a [ | 1CNU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_polyphaga Acanthamoeba polyphaga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNU OCA]. | ||
==Reference== | ==Reference== | ||
Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin., Blanchoin L, Pollard TD, J Biol Chem. 1998 Sep 25;273(39):25106-11. PMID:[http:// | Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin., Blanchoin L, Pollard TD, J Biol Chem. 1998 Sep 25;273(39):25106-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9737968 9737968] | ||
[[Category: Acanthamoeba polyphaga]] | [[Category: Acanthamoeba polyphaga]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: contractile]] | [[Category: contractile]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:26:42 2008'' |
Revision as of 11:26, 20 March 2008
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, resolution 2.25Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA
OverviewOverview
Acanthamoeba actophorin is a member of ADF/cofilin family that binds both actin monomers and filaments. We used fluorescence anisotropy to study the interaction of actin monomers with recombinant actophorin labeled with rhodamine on a cysteine substituted for Serine-88. Labeled actophorin retains its affinity for actin and ability to reduce the low shear viscosity of actin filaments. At physiological ionic strength, actophorin binds Mg-ADP-actin monomers (Kd = 0.1 microM) 40 times stronger than Mg-ATP-actin monomers. When bound to actin monomers, actophorin has no effect on elongation at either end of actin filaments by Mg-ATP-actin and slightly increases the rate of elongation at both ends by Mg-ADP-actin. Thus actophorin does not sequester actin monomers. Sedimentation equilibrium ultracentrifugation shows that actophorin and profilin compete for binding actin monomers. Actophorin and profilin have opposite effects on the rate of exchange of nucleotide bound to actin monomers. Despite the high affinity of actophorin for ADP-actin, physiological concentrations of profilin overcome the inhibition of ADP exchange by actophorin. Profilin rapidly recycles ADP-actin back to the profilin-ATP-actin pool ready for elongation of actin filaments.
About this StructureAbout this Structure
1CNU is a Single protein structure of sequence from Acanthamoeba polyphaga. Full crystallographic information is available from OCA.
ReferenceReference
Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin., Blanchoin L, Pollard TD, J Biol Chem. 1998 Sep 25;273(39):25106-11. PMID:9737968
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