Primary structure of streptococcal Pep M5 protein: Absence of extensive sequence repeats
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چکیده
منابع مشابه
Presence of two distinct regions in the coiled-coil structure of the streptococcal Pep M5 protein: relationship to mammalian coiled-coil proteins and implications to its biological properties.
The complete amino acid sequence of Pep M5, a biologically active 197-residue fragment comprising nearly half of the group A streptococcal M5 protein, has structural features characteristic of an alpha-helical coiled-coil protein. Fourier analyses of the nonpolar residues show strong periodicities based on repeats of 7 residues (7/2 and 7/3). Except for the nonhelical NH2-terminal 12-residue se...
متن کاملANTIGENIC DOMAINS OF STREPTOCOCCAL Pep
M protein of the group A streptococcus is an elongated, alpha-helical coiledcoil molecule that extends from the bacterial cell surface as a flexible fibrillar structure (1, 2). It is a major virulence factor for the bacteria, by virtue of its property of impeding the phagocytosis of the organisms (3). >75 serologically distinct variants of the M protein have been recognized over the years and, ...
متن کاملThe complete amino acid sequence of a biologically active 197-residue fragment of M protein isolated from type 5 group A streptococci.
The complete amino acid sequence of a peptic fragment (Pep M5) of the group A streptococcal type 5 M protein, the antiphagocytic cell surface molecule of the bacteria, is described. This fragment, comprising nearly half of the native M molecule, is biologically active in that it has the ability to interact with opsonic antibodies as well as to evoke such an antibody response in rabbits. The seq...
متن کاملAntigenic domains of the streptococcal Pep M5 protein. Localization of epitopes crossreactive with type 6 M protein and identification of a hypervariable region of the M molecule
Pep M5, the pepsin-derived N-terminal half of the group A streptococcal type 5 M protein exhibits immunologic crossreaction with type 6 M protein, localizing some of the M6-crossreactive epitope(s) within this segment of the M5 protein. Based on the amino acid sequence of the Pep M5 protein, two structurally distinct domains have been recognized within its coiled-coil structure. We have now fou...
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Peroxidase enzymes are vastly applicable in industry and diagnosiss. Recently, we introduced a new kind of peroxidase gene from Lepidium draba (LDP). According to protein multiple sequence alignment results, LDP had 93% similarity and 88.96% identity with horseradish peroxidase C1A (HRP C1A). In the current study we employed in silico tools to determine, to which group of peroxidase enzymes LDP...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1983
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.80.18.5475