NMR structure of the hypothetical protein NMA1147 from Neisseria meningitidis reveals a distinct 5-helix bundle.
نویسندگان
چکیده
Gaohua Liu, Dinesh K. Sukumaran, Duanxiang Xu, Yiwen Chiang, Thomas Acton, Sharon Goldsmith-Fischman, Barry Honig, Gaetano T. Montelione, and Thomas Szyperski* Department of Chemistry, University at Buffalo, the State University of New York, Buffalo, New York Center of Advanced Biotechnology and Medicine and Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York Northeast Structural Genomics Consortium
منابع مشابه
In silico Analysis and Modeling of ACP-MIP–PilQ Chimeric Antigen from Neisseria meningitidis Serogroup B
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Neisseria meningitidis is a major causative agent of bacterial septicemia and meningitis in humans. Currently, there are no vaccines to prevent disease caused by strains of N.meningitidis serogroup B. The Class 1 Outer Membrane Protein (OMP) has been named porA which is a cation selective transmembrane protein of 45 KDa that forms trimeric pore in the meningococcal outer membrane. PorA from ser...
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Neisseria meningitidis is a facultative pathogen bacterium which is well founded with a number of adhesion molecules to facilitate its colonization in human nasopharynx track. Neisseria meningitidis is a major cause of mortality from sever meningococcal disease and septicemia. The Neisseria meningitidis adhesion, NadA, is a trimeric autotransporter adhesion molecule which is involved in cell ad...
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ورودعنوان ژورنال:
- Proteins
دوره 55 3 شماره
صفحات -
تاریخ انتشار 2004