Streptococcal Scl1 and Scl2 Proteins Form Collagen-like Triple Helices
نویسندگان
چکیده
منابع مشابه
Combinatorial search for the ligands that specifically recognize the streptococcal collagen-like proteins Scl1 and Scl2
Phage-encoded peptide libraries are often used to study biomolecular interactions. We employed this combinatorial approach to identify ligands specific for the streptococcal collagen-like proteins, Scl1 and Scl2, which are expressed on the cell surface by group A Streptococcus. Several sequence motifs displayed by phages were selected for their binding ability to different Scl variants. D 2005 ...
متن کاملUnique Footprint in the scl1.3 Locus Affects Adhesion and Biofilm Formation of the Invasive M3-Type Group A Streptococcus
The streptococcal collagen-like proteins 1 and 2 (Scl1 and Scl2) are major surface adhesins that are ubiquitous among group A Streptococcus (GAS). Invasive M3-type strains, however, have evolved two unique conserved features in the scl1 locus: (i) an IS1548 element insertion in the scl1 promoter region and (ii) a nonsense mutation within the scl1 coding sequence. The scl1 transcript is drastica...
متن کاملSelf-assembly of synthetic collagen triple helices.
Collagen is the most abundant protein in animals and the major component of connective tissues. Although collagen isolated from natural sources has long served as the basis for some biomaterials, natural collagen is difficult to modify and can engender pathogenic and immunological side effects. Collagen comprises a helix of three strands. Triple helices derived from synthetic peptides are much ...
متن کاملMolecular stability of chemically modified collagen triple helices.
Ionic residues influence the stability of collagen triple helices and play a relevant role in the spontaneous aggregation of fibrillar collagens. Collagen types I and II and some of their CNBr peptides were chemically modified in mild conditions with two different protocols. Primary amino groups of Lys and Hyl were N-methylated by formaldehyde in reducing conditions or N-acetylated by sulfosucc...
متن کاملPeptide tessellation yields micron-scale collagen triple helices
Sticky-ended DNA duplexes can associate spontaneously into long double helices; however, such self-assembly is much less developed with proteins. Collagen is the most prevalent component of the extracellular matrix and a common clinical biomaterial. As for natural DNA, the ~103-residue triple helices (~300 nm) of natural collagen are recalcitrant to chemical synthesis. Here we show how the self...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2002
ISSN: 0021-9258
DOI: 10.1074/jbc.m201163200