Source:http://linkedlifedata.com/resource/pubmed/id/21049953
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
47
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| pubmed:dateCreated |
2010-11-24
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| pubmed:abstractText |
The selective binding between avian and human influenza A viral hemagglutinins (HA) subtype H3 and Neu5Ac?2-3 and ?2-6Gal (avian ?2-3, human ?2-6) is qualitatively rationalized by the fragment molecular orbital (FMO) method. We suggest a general model of analyzing protein-ligand interactions based on the electrostatic, polarization, dispersion, and desolvation components obtained from quantum-mechanical calculations at the MP2/6-31G(d) level with the polarizable continuum model of solvation. The favorable avian H3 (A/duck/Ukraine/1963)-avian ?2-3 binding arises from the hydrophilic interaction between Gal-4 OH and side-chain NH(2)CO on Gln226, which is supported by the intermolecular hydrogen-bond network to the 1-COO group on Neu5Ac moiety. A substitution of Gln226Leu in the avian H3 HA1 domain increases the binding affinity to human ?2-6 due to the Leu226···human ?2-6 dispersion with a small entropic penalty during the complex formation. The remarkable human H3 (A/Aichi/2/1968)-human ?2-6 binding is not governed by the Ser228-OH···OH-9 Neu5Ac hydrogen bond. These fragment-based chemical aspects can help design monovalent inhibitors of the influenza viral HA-sialoside binding and the simulation studies on the viral HAs-human ?2-6 binding.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Gases,
http://linkedlifedata.com/resource/pubmed/chemical/Hemagglutinin Glycoproteins...,
http://linkedlifedata.com/resource/pubmed/chemical/Mutant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sialic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Water,
http://linkedlifedata.com/resource/pubmed/chemical/hemagglutinin, avian influenza A...,
http://linkedlifedata.com/resource/pubmed/chemical/hemagglutinin, human influenza A...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
1520-5126
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
1
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| pubmed:volume |
132
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
16862-72
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| pubmed:meshHeading |
pubmed-meshheading:21049953-Animals,
pubmed-meshheading:21049953-Gases,
pubmed-meshheading:21049953-Hemagglutinin Glycoproteins, Influenza Virus,
pubmed-meshheading:21049953-Humans,
pubmed-meshheading:21049953-Influenza A Virus, H3N2 Subtype,
pubmed-meshheading:21049953-Influenza A Virus, H3N8 Subtype,
pubmed-meshheading:21049953-Influenza A virus,
pubmed-meshheading:21049953-Models, Molecular,
pubmed-meshheading:21049953-Mutant Proteins,
pubmed-meshheading:21049953-Mutation,
pubmed-meshheading:21049953-Protein Binding,
pubmed-meshheading:21049953-Protein Stability,
pubmed-meshheading:21049953-Protein Structure, Tertiary,
pubmed-meshheading:21049953-Quantum Theory,
pubmed-meshheading:21049953-Sialic Acids,
pubmed-meshheading:21049953-Substrate Specificity,
pubmed-meshheading:21049953-Thermodynamics,
pubmed-meshheading:21049953-Water
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| pubmed:year |
2010
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| pubmed:articleTitle |
Role of the key mutation in the selective binding of avian and human influenza hemagglutinin to sialosides revealed by quantum-mechanical calculations.
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| pubmed:affiliation |
Nanosystem Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan. sawada-t@aist.go.jp
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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