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Title
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Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation.
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Authors
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N.M.Mahoney,
P.A.Janmey,
S.C.Almo.
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Ref.
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Nat Struct Biol, 1997,
4,
953-960.
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PubMed id
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Abstract
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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 A 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.
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