PDBsum entry: 1bhd

Structural protein

PDB id: 1bhd

Contents

Protein chains

108 a.a. *

Waters ×173

* Residue conservation analysis

PDB id:

1bhd

Name:

Structural protein

Title:

Second calponin homology domain from utrophin

Structure:

Utrophin. Chain: a, b. Fragment: 2nd calponin homology domain from actin binding region. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Cell_line: bl21. Organ: plasma. Tissue: muscle. Cellular_location: links cytoskeleton to plasma membrane. Gene: utrn, dmdl. Expressed in: escherichia coli bl21(de3).

Resolution:

2.00Å R-factor: 0.202 R-free: 0.257

Authors:

N.H.Keep,S.J.Winder,J.Kendrick-Jones

Key ref:

N.H.Keep et al. (1999). The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin. J Mol Biol, 285, 1257-1264. PubMed id: 9887274 DOI: 10.1006/jmbi.1998.2406

Date:

05-Jun-98 Release date: 13-Jan-99

Protein chains

P46939  (UTRO_HUMAN) -  Utrophin

Seq: 3433 a.a.

Struc: 108 a.a.*

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

DOI no: 10.1006/jmbi.1998.2406

J Mol Biol 285:1257-1264 (1999)

PubMed id: 9887274

The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin.

N.H.Keep, F.L.Norwood, C.A.Moores, S.J.Winder, J.Kendrick-Jones.

ABSTRACT

Utrophin is a close homologue of dystrophin, the protein defective in Duchenne muscular dystrophy. Like dystrophin, it is composed of three regions: an N-terminal region that binds actin filaments, a large central region with triple coiled-coil repeats, and a C-terminal region that interacts with components in the dystroglycan protein complex at the plasma membrane. The N-terminal actin-binding region consists of two calponin homology domains and is related to the actin-binding domains of a superfamily of proteins including alpha-actinin, spectrin and fimbrin. Here, we present the 2.0 A structure of the second calponin homology domain of utrophin solved by X-ray crystallography, and compare it to the other calponin homology domains previously determined from spectrin and fimbrin.

Selected figure(s)

Figure 2.
Figure 2. The structure of utrophin CH2 domain with helices labelled as in Figure 3. The region corresponding to ABS3 is in green. The upper and lower views differ by a 90 ° rotation around the vertical axis. The Figure was drawn with MOLSCRIPT (Kraulis, 1991).

Figure 3.
Figure 3. Aligned sequences of the four CH domains with solved structures based on the 3D superposition used for Figure 4. The position of the helices in utrophin CH2 domain are marked and these are labelled using both the a1-a6 scheme of the fimbrin structure (Goldsmith et al., 1997) and with the A-G scheme of the spectrin CH2 domain (Carugo et al., 1997). The position of ABS1 and ABS2, which are found in the CH1 domain of the actin-binding region, are marked below the fimbrin CH1.1 domain sequence. ABS3 is marked above the three CH2 domain sequences. The Figure was drawn with ALSCRIPT (Barton, 1993).

The above figures are reprinted by permission from Elsevier: J Mol Biol (1999, 285, 1257-1264) copyright 1999.

Figures were selected by the author.