From the first to the second domain of gelsolin: A common path on the surface of actin?

Edward Irobi, Leslie D. Burtnick, Dunja Urosev, Kartik Narayan, Robert C. Robinson

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)


We present the 2.6 Å resolution crystal structure of a complex formed between G-actin and gelsolin fragment Met25-Gln160 (G1+). The structure differs from those of other gelsolin domain 1 (G1) complexes in that an additional six amino acid residues from the crucial linker region into gelsolin domain 2 (G2) are visible and are attached securely to the surface of actin. The linker segment extends away from G1 up the face of actin in a direction that infers G2 will bind along the same long-pitch helical strand as the actin bound to G1. This is consistent with a mechanism whereby G2 attaches gelsolin to the side of a filament and then directs G1 toward a position where it would disrupt actin-actin contacts. Alignment of the sequence of the structurally important residues within the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin β4) suggests that the opposing activities of filament assembly and disassembly may exploit a common patch on the surface of actin.

Original languageEnglish
Pages (from-to)86-90
Number of pages5
JournalFEBS Letters
Issue number2-3
Publication statusPublished - Sept 25 2003
Externally publishedYes


  • Actin
  • Crystal structure
  • Gelsolin
  • WH2 domain

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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