PDBsum entry 1cf0

Complex (actin-binding protein/peptide)

PDB id: 1cf0

Contents

Protein chain

138 a.a. *

Ligands

PRO-PRO-PRO-PRO-PRO-PRO-PRO-PRO-IYR

Waters ×39

* Residue conservation analysis

PDB id:

1cf0

Name:

Complex (actin-binding protein/peptide)

Title:

Human platelet profilin complexed with an l-pro10-iodotyrosine peptide

Structure:

Protein (profilin). Chain: a, b. Engineered: yes. Protein (l-pro10-iodotyrosine). Chain: c. Engineered: yes. Other_details: poly-proline-peptide linked to iodo-tyrosine residue

Source:

Homo sapiens. Human. Organism_taxid: 9606. Tissue: platelet. Cellular_location: cytoplasm. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Other_details: synthetic. Synthetic: yes.

Biol. unit:

Trimer (from PQS)

Resolution:

2.20Å R-factor: 0.210 R-free: 0.310

Authors:

D.A.Rozwarski,N.M.Mahoney,S.C.Almo

Key ref:

N.M.Mahoney et al. (1999). Profilin binds proline-rich ligands in two distinct amide backbone orientations. Nat Struct Biol, 6, 666-671. PubMed id: 10404225 DOI: 10.1038/10722

Date:

23-Mar-99 Release date: 06-Jul-99

Protein chains

P07737  (PROF1_HUMAN) -  Profilin-1 from Homo sapiens

Seq: 140 a.a.

Struc: 138 a.a.

DOI no: 10.1038/10722

Nat Struct Biol 6:666-671 (1999)

PubMed id: 10404225

Profilin binds proline-rich ligands in two distinct amide backbone orientations.

N.M.Mahoney, D.A.Rozwarski, E.Fedorov, A.A.Fedorov, S.C.Almo.

ABSTRACT

The actin regulatory protein profilin is targeted to specific cellular regions through interactions with highly proline-rich motifs embedded within its binding partners. New X-ray crystallographic results demonstrate that profilin, like SH3 domains, can bind proline-rich ligands in two distinct amide backbone orientations. By further analogy with SH3 domains, these data suggest that non-proline residues in profilin ligands may dictate the polarity and register of binding, and the detailed organization of the assemblies involving profilin. This degeneracy may be a general feature of modules that bind proline-rich ligands, including WW and EVH1 domains, and has implications for the assembly and activity of macromolecular complexes involved in signaling and the regulation of the actin cytoskeleton.

Selected figure(s)

Figure 1.
Figure 1. Proline-rich sequences in proteins implicated in profilin binding through genetic and/or biochemical studies. Profilin has been shown to interact directly with VASP^17, Mena^15, Bni1p^18, and cdc12p^19, and with Capuccino^24 in genetic screens.

Figure 3.
Figure 3. Electron density of the HMC-L-Pro[15] peptide and the asymmetric unit of the HPP−HMC-L-Pro[15] complex. a, Refined HMC-L-Pro[15] coordinates with 2.3 Å 2F[o] - F[c] electron density (blue). Peptide orientation was unambiguously defined by density corresponding to the N-terminal HMC moiety. The five aromatic residues that comprise the proline-rich peptide binding core and three additional residues from the extended binding site are highlighted in red. b, The asymmetric unit of the HPP−HMC-L-Pro[15] crystal contains two HPP−peptide complexes related by two-fold non-crystallographic symmetry. The five aromatic residues that define the minimal poly-L-proline binding site are shown in red for HPP-1. This figure was generated using SETOR^31.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (1999, 6, 666-671) copyright 1999.

Figures were selected by an automated process.