1cnu: Difference between revisions

Revision as of 20:59, 30 June 2008

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File:1cnu.png

Template:STRUCTURE 1cnu

PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGAPHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA

Template:ABSTRACT PUBMED 9737968

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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-'''PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9737968}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9737968 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9737968}}
 ==About this Structure==
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 [[Category: Cofilin]]
 [[Category: Contractile]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:55:54 2008''
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