Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation

Nicole M. Mahoney, Paul A. Janmey, Steven C. Almo

Research output: Contribution to journalArticle

129 Citations (Scopus)

Abstract

Profilin, a ubiquitous low molecular weight (13,000-15,000 M(r)) actin binding protein, regulates the formation of F-actin structures in vivo, and is localized to specific cellular regions through interaction with proline- rich sequences. Here we report the 2.2 Å X-ray structure of the complex between human platelet profilin (HPP) and a decamer of L-proline (L-Pro10). The L-Pro10 peptide adopts a left-handed type II poly-L-proline helix (PPiI) and binds to a highly conserved patch of aromatic amino acids on the surface of profilin. The peptide and actin binding sites reside on orthogonal surfaces, and L-Pro10 binding does not result in a conformational rearrangement of HPP. This structure suggests a mechanism for the localization of profilin and its actin-related activities to sites of actin filament assembly in vivo.

Original languageEnglish (US)
Pages (from-to)953-960
Number of pages8
JournalNature Structural Biology
Volume4
Issue number11
DOIs
StatePublished - 1997

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Profilins
Morphogenesis
Actins
Platelets
Proline
Blood Platelets
Microfilament Proteins
Aromatic Amino Acids
Actin Cytoskeleton
Molecular Weight
Molecular weight
Binding Sites
X-Rays
polyproline
X rays
Peptides

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation. / Mahoney, Nicole M.; Janmey, Paul A.; Almo, Steven C.

In: Nature Structural Biology, Vol. 4, No. 11, 1997, p. 953-960.

Research output: Contribution to journalArticle

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