DC Field | Value | Language |
---|---|---|
dc.contributor.author | S.T. Kim | ko |
dc.contributor.author | Byun, Si Myung | ko |
dc.date.accessioned | 2013-02-28T02:43:29Z | - |
dc.date.available | 2013-02-28T02:43:29Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2000-02 | - |
dc.identifier.citation | JOURNAL OF BIOCHEMISTRY, v.128, no.3, pp.449 - 454 | - |
dc.identifier.issn | 0021-924X | - |
dc.identifier.uri | http://hdl.handle.net/10203/72351 | - |
dc.description.abstract | We designed and expressed a single-chain class II major histocompatibility complex molecule capable of forming a stable complex with an antigenic peptide. The peptide-binding preference of the single-chain (sc) human leukocyte antigen derived from DRB5*0101 (DR51) was determined to be similar to that of the authentic one, which requires a bulky hydrophobic residue at position-1 (P1) as a primary anchor. For modulation of the peptide-binding affinity, we modified binding pocket 1 of sc DR51 by site-directed mutagenesis, The relative binding affinity of the engineered sc DR51 for several P1-substituted peptides was measured by competition assaying with a fluorescence labeled peptide. The sc DR51 molecule showed high affinity to the self-peptide derived from myelin basic protein, 87-98 with Phe as the P1 residue (F90F). While reduction of pocket 1 volume (beta G86V) decreased the affinity of F90F, it rather increased the affinity of the Ala-substituted peptide as to the P1 residue (F90A), Through more extensive engineering in the peptide-binding groove of the sc DR51 molecule, it is expected that we can construct sc DR51 variants with various peptide ligand motifs. | - |
dc.language | English | - |
dc.publisher | Oxford Univ Press | - |
dc.subject | MHC CLASS-II | - |
dc.subject | PROTEIN HLA-DR1 | - |
dc.subject | CRYSTAL-STRUCTURES | - |
dc.subject | MYASTHENIA-GRAVIS | - |
dc.subject | T-CELLS | - |
dc.subject | MOLECULES | - |
dc.subject | ANTIGEN | - |
dc.subject | MOTIFS | - |
dc.subject | IDENTIFICATION | - |
dc.subject | APOPTOSIS | - |
dc.title | Modulation of the Peptide-Binding Specificity of a Single-Chain Class II Major Histocompatibility Complex | - |
dc.type | Article | - |
dc.identifier.wosid | 000089147000015 | - |
dc.identifier.scopusid | 2-s2.0-0033819226 | - |
dc.type.rims | ART | - |
dc.citation.volume | 128 | - |
dc.citation.issue | 3 | - |
dc.citation.beginningpage | 449 | - |
dc.citation.endingpage | 454 | - |
dc.citation.publicationname | JOURNAL OF BIOCHEMISTRY | - |
dc.contributor.nonIdAuthor | S.T. Kim | - |
dc.type.journalArticle | Article | - |
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