Minimum folding unit of dystrophin rod domain.


Abstract

Fragments of the rod domain of dystrophin, which consists of spectrin-like repeating sequences, have been prepared by expression in Escherichia coli. The phasing established earlier for the dystrophin rod, as well as for Drosophila spectrin and smooth muscle alpha-actinin, suggested a length of less than 113 residues for the dystrophin repeat that we have chosen. Fragments with a common N-terminus and lengths between 113 and 119 residues were prepared. The formation of the stable native tertiary fold could be recognized by resistance to proteolysis, the circular dichroism spectrum in the regions of both peptide and aromatic absorption bands and the resolution of the long-wavelength component in the tryptophan absorption spectrum. It was found that the critical length for folding was 117 residues: shortening the chain by 1 further residue resulted in loss of the capacity to form a defined tertiary structure. Residue 117 is a glutamine; replacement of this by a methionine residue did not impair the ability of the chain to enter the folded conformation, implying that it is the length of the C-terminal alpha-helix, rather than any specific side-chain interaction, that is critical in determining the stability of the native structure. The fragment of 119 residues forms a significantly more stable structure than that of 117. It appears that the minimum unit capable of forming the native fold extends some residues into the adjoining sequence repeat. Study holds ProTherm entries: 5078, 5079 Extra Details: fragments; native tertiary fold; alpha-helix;,specific side-chain interaction

Submission Details

ID: N3iGcEv

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:28 p.m.

Version: 1

Publication Details
Kahana E;Gratzer WB,Biochemistry (1995) Minimum folding unit of dystrophin rod domain. PMID:7794924
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
1EG4 2000-08-23 2.0 STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE
1EG3 2000-08-23 2.0 STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE
3UUN 2012-09-19 2.3 Crystal Structure of N-terminal first spectrin repeat of dystrophin
1DXX 2000-05-16 2.6 N-terminal Actin-binding Domain of Human Dystrophin

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
96.2 Dystrophin Q5GN48 DMD_PIG
98.0 Dystrophin O97592 DMD_CANLF
100.0 Dystrophin P11532 DMD_HUMAN
94.7 Dystrophin P11530 DMD_RAT
95.5 Dystrophin P11531 DMD_MOUSE