Literature DB >> 7447789

Influenza virus haemagglutinin. Structural predictions suggest that the fibrillar appearance is due to the presence of a coiled-coil.

C W Ward, T A Dopheide.   

Abstract

Predictions of secondary structure for the two chains HA1 and HA2 of the haemagglutinin from the Hong Kong influenza virus A/Memphis/102/72 reveal a striking contrast between the potential conformations of the two chains. HA1 is predicted to be rich in beta-structure while HA2 is highly helical. The predictions further suggest that coiled-coil type interactions between the central helical segments of the HA2 chains may hold the haemagglutinin monomers together in the virus.

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Year:  1980        PMID： 7447789     DOI： 10.1071/bi9800441

Source DB:  PubMed          Journal:  Aust J Biol Sci        ISSN： 0004-9417


  10 in total

1.  Primary structure of streptococcal Pep M5 protein: Absence of extensive sequence repeats.

Authors:  B N Manjula; S M Mische; V A Fischetti
Journal:  Proc Natl Acad Sci U S A       Date:  1983-09       Impact factor: 11.205

2.  Structural characterization of an early fusion intermediate of influenza virus hemagglutinin.

Authors:  Rui Xu; Ian A Wilson
Journal:  J Virol       Date:  2011-03-02       Impact factor: 5.103

3.  Studies using double mutants of the conformational transitions in influenza hemagglutinin required for its membrane fusion activity.

Authors:  D A Steinhauer; J Martín; Y P Lin; S A Wharton; M B Oldstone; J J Skehel; D C Wiley
Journal:  Proc Natl Acad Sci U S A       Date:  1996-11-12       Impact factor: 11.205

4.  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.

Authors:  B N Manjula; B L Trus; V A Fischetti
Journal:  Proc Natl Acad Sci U S A       Date:  1985-02       Impact factor: 11.205

5.  A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation.

Authors:  J Chen; S A Wharton; W Weissenhorn; L J Calder; F M Hughson; J J Skehel; D C Wiley
Journal:  Proc Natl Acad Sci U S A       Date:  1995-12-19       Impact factor: 11.205

6.  Primary and secondary structure of hamster vimentin predicted from the nucleotide sequence.

Authors:  Y E Quax-Jeuken; W J Quax; H Bloemendal
Journal:  Proc Natl Acad Sci U S A       Date:  1983-06       Impact factor: 11.205

7.  Intermonomer Interactions in Hemagglutinin Subunits HA1 and HA2 Affecting Hemagglutinin Stability and Influenza Virus Infectivity.

Authors:  Wei Wang; Christopher J DeFeo; Esmeralda Alvarado-Facundo; Russell Vassell; Carol D Weiss
Journal:  J Virol       Date:  2015-08-12       Impact factor: 5.103

8.  Structures of complexes formed by H5 influenza hemagglutinin with a potent broadly neutralizing human monoclonal antibody.

Authors:  Xiaoli Xiong; Davide Corti; Junfeng Liu; Debora Pinna; Mathilde Foglierini; Lesley J Calder; Stephen R Martin; Yi Pu Lin; Philip A Walker; Patrick J Collins; Isabella Monne; Amorsolo L Suguitan; Celia Santos; Nigel J Temperton; Kanta Subbarao; Antonio Lanzavecchia; Steven J Gamblin; John J Skehel
Journal:  Proc Natl Acad Sci U S A       Date:  2015-07-13       Impact factor: 11.205

9.  Vale Colin Ward-A Leader in Receptor Structural Biology.

Authors:  Michael C Lawrence; Peter M Colman
Journal:  Front Endocrinol (Lausanne)       Date:  2017-05-11       Impact factor: 5.555

10.  Specific single or double proline substitutions in the "spring-loaded" coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity.

Authors:  H Qiao; S L Pelletier; L Hoffman; J Hacker; R T Armstrong; J M White
Journal:  J Cell Biol       Date:  1998-06-15       Impact factor: 10.539
  10 in total

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