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'''STRUCTURE OF INFLUENZA HAEMAGGLUTININ AT THE PH OF MEMBRANE FUSION'''<br />
'''STRUCTURE OF INFLUENZA HAEMAGGLUTININ AT THE PH OF MEMBRANE FUSION'''<br />
==Overview==
==Overview==
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Low pH induces a conformational change in the influenza virus, haemagglutinin, which then mediates fusion of the viral and host cell, membranes. The three-dimensional structure of a fragment of the, haemagglutinin in this conformation reveals a major refolding of the, secondary and tertiary structure of the molecule. The apolar fusion, peptide moves at least 100 A to one tip of the molecule. At the other end, a helical segment unfolds, a subdomain relocates reversing the chain, direction, and part of the structure becomes disordered.
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Low pH induces a conformational change in the influenza virus haemagglutinin, which then mediates fusion of the viral and host cell membranes. The three-dimensional structure of a fragment of the haemagglutinin in this conformation reveals a major refolding of the secondary and tertiary structure of the molecule. The apolar fusion peptide moves at least 100 A to one tip of the molecule. At the other end a helical segment unfolds, a subdomain relocates reversing the chain direction, and part of the structure becomes disordered.
==About this Structure==
==About this Structure==
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1HTM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Uncultured_beta_proteobacterium_umtra-608 Uncultured beta proteobacterium umtra-608]. The following page contains interesting information on the relation of 1HTM with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb76_1.html Hemagglutinin]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HTM OCA].
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1HTM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Uncultured_beta_proteobacterium_umtra-608 Uncultured beta proteobacterium umtra-608]. The following page contains interesting information on the relation of 1HTM with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb76_1.html Hemagglutinin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTM OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Uncultured beta proteobacterium umtra-608]]
[[Category: Uncultured beta proteobacterium umtra-608]]
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[[Category: Bullough, P.A.]]
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[[Category: Bullough, P A.]]
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[[Category: Hughson, F.M.]]
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[[Category: Hughson, F M.]]
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[[Category: Skehel, J.J.]]
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[[Category: Skehel, J J.]]
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[[Category: Wiley, D.C.]]
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[[Category: Wiley, D C.]]
[[Category: influenza virus hemagglutinin]]
[[Category: influenza virus hemagglutinin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:01:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:41 2008''

Revision as of 11:04, 21 February 2008


1htm, resolution 2.5Å

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STRUCTURE OF INFLUENZA HAEMAGGLUTININ AT THE PH OF MEMBRANE FUSION

Overview

Low pH induces a conformational change in the influenza virus haemagglutinin, which then mediates fusion of the viral and host cell membranes. The three-dimensional structure of a fragment of the haemagglutinin in this conformation reveals a major refolding of the secondary and tertiary structure of the molecule. The apolar fusion peptide moves at least 100 A to one tip of the molecule. At the other end a helical segment unfolds, a subdomain relocates reversing the chain direction, and part of the structure becomes disordered.

About this Structure

1HTM is a Protein complex structure of sequences from Uncultured beta proteobacterium umtra-608. The following page contains interesting information on the relation of 1HTM with [Hemagglutinin]. Full crystallographic information is available from OCA.

Reference

Structure of influenza haemagglutinin at the pH of membrane fusion., Bullough PA, Hughson FM, Skehel JJ, Wiley DC, Nature. 1994 Sep 1;371(6492):37-43. PMID:8072525

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