Expression and disulfide-bond connectivity of the second ligand-binding repeat of the human LDL receptor

Bieri S., Djordjevic J.T., Jamshidi N., Smith R. and Kroon P.A. (1995) Expression and disulfide-bond connectivity of the second ligand-binding repeat of the human LDL receptor. FEBS Letters, 371 3: 341-344. doi:10.1016/0014-5793(95)00939-7


Author Bieri S.
Djordjevic J.T.
Jamshidi N.
Smith R.
Kroon P.A.
Title Expression and disulfide-bond connectivity of the second ligand-binding repeat of the human LDL receptor
Journal name FEBS Letters   Check publisher's open access policy
ISSN 0014-5793
Publication date 1995-09-11
Sub-type Article (original research)
DOI 10.1016/0014-5793(95)00939-7
Volume 371
Issue 3
Start page 341
End page 344
Total pages 4
Subject 1303 Specialist Studies in Education
1304 Biophysics
1307 Cell Biology
1311 Genetics
1312 Molecular Biology
1315 Structural Biology
Abstract The human LDL receptor (LDLR) has a binding domain which consists of seven contiguous ligand-binding (LB) repeats, each ∼40 amino acids long with three disulfide bonds. The second LB repeat, which is required for full binding of LDL, has been expressed, purified and folded to yield a single, fully oxidized isomer. By selective reduction and alkylation, we have shown that the cysteine residues have a I-III, II-V, IV-VI connectivity, matching that recently determined for the amino-terminal repeat. We suggest that the first two LB repeats of the LDLR, with their unique disulfide-bonding pattern, serve as a structural paradigm for other LB repeats.
Keyword Disulfide
Expression
LDL receptor
Mass spectrometry
Peptide
TCEP
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import
 
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