The relative importance of individual DR binding motif positions as defined by peptide anchor analysis of influenza hemagglutinin peptide 306-318 and human myelin basic protein peptide 152-165 binding to several DR molecules: definition of a common extended DR binding motif.

Posch, P E; Hastings, A E; Rosen-Bronson, S; Richert, J R; Hurley, C K

Posch, P E; Hastings, A E; Rosen-Bronson, S; Richert, J R; Hurley, C K.

Affiliation

Posch PE; Department of Microbiology and Immunology, Georgetown University Medical Center, Washington 20007, USA.

Eur J Immunol ; 26(8): 1884-91, 1996 Aug.

Article in En | MEDLINE | ID: mdl-8765035

Subject(s)

HLA-DR Antigens/chemistry; Hemagglutinins, Viral/chemistry; Influenza A virus/chemistry; Myelin Basic Protein/chemistry; Peptide Fragments/chemistry; Protein Conformation; Amino Acid Sequence; Cell Line; HLA-DR Antigens/genetics; HLA-DR Antigens/metabolism; Hemagglutinins, Viral/genetics; Hemagglutinins, Viral/metabolism; Humans; Influenza A virus/genetics; Influenza A virus/metabolism; Models, Molecular; Molecular Sequence Data; Myelin Basic Protein/genetics; Myelin Basic Protein/metabolism; Peptide Fragments/metabolism; Protein Binding/immunology; Transfection/immunology

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Collection: 01-internacional Database: MEDLINE Main subject: Influenza A virus / Peptide Fragments / Protein Conformation / HLA-DR Antigens / Myelin Basic Protein / Hemagglutinins, Viral Limits: Humans Language: En Journal: Eur J Immunol Year: 1996 Document type: Article Affiliation country: United States Country of publication: Germany

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