z-logo
open-access-imgOpen Access
Influenza A Virus N5 Neuraminidase Has an Extended 150-Cavity
Author(s) -
Mingyang Wang,
Jianxun Qi,
Yue Liu,
Christopher J. Vavricka,
Yan Wu,
Qing Li,
George F. Gao
Publication year - 2011
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.00638-11
Subject(s) - neuraminidase , biology , serotype , virology , residue (chemistry) , virus , influenza a virus , microbiology and biotechnology , biochemistry
There are 9 serotypes of neuraminidase (NA) from influenza A virus (N1 to N9), which are classified into two groups based on primary sequences (groups 1 and 2). The structural hallmark of the two groups is the presence or absence of an extra 150-cavity (formed by the 150-loop) in the active site. Thus far, structures of NAs from 6 out of the 9 serotypes have been solved. Here, we solved the N5 structure, the last unknown structure group 1 serotype with a unique Asn147 residue in its 150-loop, demonstrating that it has an extended 150-cavity that closes upon inhibitor binding.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom