1cnu
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1cnu.gif|left|200px]] | [[Image:1cnu.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1cnu", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | | | + | or leave the SCENE parameter empty for the default display. |
- | | | + | --> |
- | + | {{STRUCTURE_1cnu| PDB=1cnu | SCENE= }} | |
- | + | ||
- | + | ||
- | }} | + | |
'''PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA''' | '''PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA''' | ||
Line 29: | Line 26: | ||
[[Category: Pollard, T D.]] | [[Category: Pollard, T D.]] | ||
[[Category: Robinson, R C.]] | [[Category: Robinson, R C.]] | ||
- | [[Category: | + | [[Category: Actin-binding protein]] |
- | [[Category: | + | [[Category: Adf]] |
- | [[Category: | + | [[Category: Cofilin]] |
- | [[Category: | + | [[Category: Contractile]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:55:54 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 09:55, 2 May 2008
PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA
Overview
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 Structure
1CNU is a Single protein structure of sequence from Acanthamoeba polyphaga. Full crystallographic information is available from OCA.
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:9737968 Page seeded by OCA on Fri May 2 12:55:54 2008