Background: Streptococcal collagen-like proteins play crucial roles in host adhesion, host cell entry, and immunomodulation of host defenses. Results: This study provides the first three-dimensional structural description of a streptococcal collagen-like protein. Conclusion: The crystal structure evidences a six-helical bundle fold, which is unusual in bacterial proteins and characteristic of viral fusion proteins. Significance: The high resolution structure provides a structural basis for the design of inhibitors of streptococcal invasion. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
The crystal structure of the streptococcal collagen-like protein 2 globular domain from invasive M3-type group a streptococcus shows significant similarity to immunomodulatory HIV protein gp41 / Squeglia, F.; Bachert, B.; De Simone, A.; Lukomski, S.; Berisio, R.. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - 289:8(2014), pp. 5122-5133. [10.1074/jbc.M113.523597]
The crystal structure of the streptococcal collagen-like protein 2 globular domain from invasive M3-type group a streptococcus shows significant similarity to immunomodulatory HIV protein gp41
Squeglia F.;De Simone A.;
2014
Abstract
Background: Streptococcal collagen-like proteins play crucial roles in host adhesion, host cell entry, and immunomodulation of host defenses. Results: This study provides the first three-dimensional structural description of a streptococcal collagen-like protein. Conclusion: The crystal structure evidences a six-helical bundle fold, which is unusual in bacterial proteins and characteristic of viral fusion proteins. Significance: The high resolution structure provides a structural basis for the design of inhibitors of streptococcal invasion. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.