A clamp-like orientation of basic residues set in a parallelogram is essential for heparin binding.
FEBS Lett
; 590(18): 3089-97, 2016 09.
Article
em En
| MEDLINE
| ID: mdl-27531580
ABSTRACT
While the majority of studies have focused on the biological roles of heparin-binding proteins, relatively little is known about their key residues and structural elements responsible for heparin interaction. In this study, we employed the IgG-binding domain B1 of Streptococcal protein G as a miniature scaffold to investigate how certain positively charged residues within the ß-sheet conformation become favorable for heparin binding. By performing a series of arginine substitution mutations followed by gain-of-heparin-binding analysis, we deduced that a clamp-like orientation with discontinuous basic residues separated by ~ 5 Å with ~ 100° interior angle is advantageous for high heparin affinity.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Heparina
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2016
Tipo de documento:
Article