PDBsum entry: 1h67

Cytoskeleton

PDB id: 1h67

Contents

Protein chain

108 a.a. *

* Residue conservation analysis

PDB id:

1h67

Name:

Cytoskeleton

Title:

Nmr structure of the ch domain of calponin

Structure:

Calponin alpha. Chain: a. Fragment: calponin homology domain, residues 28-134. Engineered: yes

Source:

Gallus gallus. Chicken. Organism_taxid: 9031. Organ: gizzard. Tissue: smooth muscle. Expressed in: escherichia coli. Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

J.Bramham,B.O.Smith,D.Uhrin,P.N.Barlow,S.J.Winder

Key ref:

J.Bramham et al. (2002). Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin:calponin. Structure, 10, 249-258. PubMed id: 11839310 DOI: 10.1016/S0969-2126(02)00703-7

Date:

07-Jun-01 Release date: 14-Feb-02

Protein chain

P26932  (CNN1_CHICK) -  Calponin-1

Seq: 292 a.a.

Struc: 108 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 

• Biological process: actomyosin structure organization (1 term)
• Biochemical function: actin binding (1 term)

DOI no: 10.1016/S0969-2126(02)00703-7

Structure 10:249-258 (2002)

PubMed id: 11839310

Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin:calponin.

J.Bramham, J.L.Hodgkinson, B.O.Smith, D.Uhrín, P.N.Barlow, S.J.Winder.

ABSTRACT

Calponin is involved in the regulation of contractility and organization of the actin cytoskeleton in smooth muscle cells. It is the archetypal member of the calponin homology (CH) domain family of actin binding proteins that includes cytoskeletal linkers such as alpha-actinin, spectrin, and dystrophin, and regulatory proteins including VAV, IQGAP, and calponin. We have determined the first structure of a CH domain from a single CH domain-containing protein, that of calponin, and have fitted the NMR-derived coordinates to the 3D-helical reconstruction of the F-actin:calponin complex using cryo-electron microscopy. The tertiary fold of this single CH domain is typical of, yet significantly different from, those of the CH domains that occur in tandem pairs to form high-affinity ABDs in other proteins. We thus provide a structural insight into the mode of interaction between F-actin and CH domain-containing proteins.

Selected figure(s)

Figure 5.
Figure 5. Side View of the Calponin CH Domain Structure Fitted to the Difference Density Map Derived from the 3D-Helical Image Reconstructions of Calponin-Decorated F-ActinThe calponin CH domain, shown as backbone trace colored as Figure 3, has been fitted into the difference density (cyan mesh): (A) in the fimbrin-like orientation [33] and (B) in the utrophin-like orientation [34]. The pointed end monomer of actin is shown in green and the barbed end monomer is in red. Distances of the closest approaches to the C[a] of labeled residues (green) in the fitted atomic model of F-actin [53] are indicated in red (Å).

The above figure is reprinted by permission from Cell Press: Structure (2002, 10, 249-258) copyright 2002.

Figure was selected by an automated process.