1w0v
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CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE SELF-PEPTIDE TIS FROM EGF-RESPONSE FACTOR 1
OverviewOverview
The F pocket of major histocompatibility complex (in humans HLA) class I, molecules accommodates the C terminus of the bound peptide. Residues, forming this pocket exhibit considerable polymorphism, and a single, difference (Asp116 in HLA-B*2705 and His116 in HLA-B*2709 heavy chains), confers differential association of these two HLA-B27 subtypes to the, autoimmune disease ankylosing spondylitis. As peptide presentation by HLA, molecules is of central importance for immune responses, we performed, thermodynamic (circular dichroism, differential scanning calorimetry, fluorescence polarization) and X-ray crystallographic analyses of both, HLA-B27 subtypes complexed with the epidermal growth factor response, factor 1-derived self-peptide TIS (RRLPIFSRL) to understand the impact of, the ... [(full description)]
About this StructureAbout this Structure
1W0V is a [Protein complex] structure of sequences from [Homo sapiens] with GOL as [ligand]. Full crystallographic information is available from [OCA].
ReferenceReference
Thermodynamic and structural equivalence of two HLA-B27 subtypes complexed with a self-peptide., Hulsmeyer M, Welfle K, Pohlmann T, Misselwitz R, Alexiev U, Welfle H, Saenger W, Uchanska-Ziegler B, Ziegler A, J Mol Biol. 2005 Mar 11;346(5):1367-79. Epub 2005 Jan 28. PMID:15713487
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