Source:http://linkedlifedata.com/resource/pubmed/id/11185954
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2001-1-19
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| pubmed:abstractText |
We have previously shown that the Saccharomyces cerevisiae cell adhesion protein alpha-agglutinin has sequence characteristics of immunoglobulin-like proteins and have successfully modeled residues 200-325, based on the structure of immunoglobulin variable-type domains. Alignments matching residues 20-200 of alpha-agglutinin with domains I and II of members of the CD2/CD4 subfamily of the immunoglobulin superfamily showed > 80% conservation of key residues despite low sequence similarity overall. Three-dimensional models of two alpha-agglutinin domains constructed on the basis of these alignments were shown to conform to peptide mapping data and biophysical properties of alpha-agglutinin. In addition, the residue volume and surface accessibility characteristics of these models resembled those of the well-packed structures of related proteins. Residue-by-residue analysis showed that packing and accessibility anomalies were largely confined to glycosylated and protease-susceptible loop regions of the domains. Surface accessibility of hydrophobic residues was typical of proteins with extensive domain interactions, a finding compatible with the hydrodynamic properties of alpha -agglutinin and the hydrophobic nature of binding to its peptide ligand alpha-agglutinin. The procedures used to align the alpha-agglutinin sequence and test the quality of the model may be applicable to other proteins, especially those that resist crystallization because of extensive glycosylation.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD2,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD4,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/mating factor
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| pubmed:status |
MEDLINE
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| pubmed:month |
Aug
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| pubmed:issn |
1521-6543
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
50
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
105-13
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:11185954-Algorithms,
pubmed-meshheading:11185954-Amino Acid Sequence,
pubmed-meshheading:11185954-Amino Acids,
pubmed-meshheading:11185954-Antigens, CD2,
pubmed-meshheading:11185954-Antigens, CD4,
pubmed-meshheading:11185954-Cell Adhesion,
pubmed-meshheading:11185954-Disulfides,
pubmed-meshheading:11185954-Glycosylation,
pubmed-meshheading:11185954-Humans,
pubmed-meshheading:11185954-Immunoglobulins,
pubmed-meshheading:11185954-Ligands,
pubmed-meshheading:11185954-Models, Biological,
pubmed-meshheading:11185954-Models, Molecular,
pubmed-meshheading:11185954-Molecular Sequence Data,
pubmed-meshheading:11185954-Peptides,
pubmed-meshheading:11185954-Protein Binding,
pubmed-meshheading:11185954-Protein Structure, Tertiary,
pubmed-meshheading:11185954-Saccharomyces cerevisiae,
pubmed-meshheading:11185954-Sequence Homology, Amino Acid,
pubmed-meshheading:11185954-Software
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| pubmed:year |
2000
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| pubmed:articleTitle |
A CD2-based model of yeast alpha-agglutinin elucidates solution properties and binding characteristics.
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| pubmed:affiliation |
Department of Biological Sciences and The Institute for Biomolecular Structure and Function, Hunter College of the City University of New York, NY 10021, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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