| First Author | Harper BD | Year | 2000 |
| Journal | Biochem J | Volume | 350 Pt 1 |
| Pages | 269-74 | PubMed ID | 10926853 |
| Mgi Jnum | J:64143 | Mgi Id | MGI:1888794 |
| Citation | Harper BD, et al. (2000) Fine mapping of the alpha-actinin binding site within cysteine-rich protein. Biochem J 350 Pt 1:269-74 |
| abstractText | The cysteine-rich proteins (CRPs) are a family of highly conserved LIM (an acronym derived from the three gene products lin-11, isl-1 and mec-3) domain proteins that have been implicated in muscle differentiation. All CRP family members characterized so far have been shown to interact with the filamentous actin cross-linker alpha-actinin. The region of CRP required for this interaction has previously been broadly mapped to the molecule's N-terminal half. Here we report that the alpha-actinin-binding region of CRP, which we have mapped by using a combination of blot overlay and Western immunoblot techniques, is confined to an 18-residue sequence occurring within the protein's N-terminal glycine-rich repeat. A site-directed mutagenesis analysis of the binding region has revealed the critical importance of a single lysine residue (lysine 65 in human CRP1). Alterations at this site lead to a 10-fold decrease in alpha-actinin binding in comparison with wild-type CRP. The critical lysine residue localizes within a short alpha-helix, raising the possibility that mutagenesis-induced alterations in alpha-actinin-binding capacity might be attributed to the disruption of a key structural element. |
