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Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). Interacting selectively and non-covalently with any protein component of any cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton). Interacting selectively and non-covalently with alpha-actinin, one of a family of proteins that cross-link F-actin as antiparallel homodimers. Alpha-actinin has a molecular mass of 93-103 KDa; at the N-terminus there are two calponin homology domains, at the C-terminus there are two EF-hands. These two domains are connected by the rod domain. This domain is formed by triple-helical spectrin repeats. Interacting selectively and non-covalently with beta-actinin, a heterodimeric actin-binding protein which caps the barbed end of actin filaments and nucleates actin polymerization in a calcium-independent manner. In myofibrils it is localized in the Z-lines. Interacting selectively and non-covalently with actinin, any member of a family of proteins that crosslink F-actin.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: actinin binding
Acc: GO:0042805
Aspect: Molecular Function
Desc: Interacting selectively and non-covalently with actinin, any member of a family of proteins that crosslink F-actin.
Proteins in PDR annotated with:
   This term: 7 [Search]
   Term or descendants: 33 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0042805 - actinin binding (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle