1dlh: Difference between revisions

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-[[Image:1dlh.gif|left|200px]]
+[[Image:1dlh.png|left|200px]]
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-==Overview==
+{{ABSTRACT_8145819}}
-An influenza virus peptide binds to HLA-DR1 in an extended conformation with a pronounced twist. Thirty-five per cent of the peptide surface is accessible to solvent and potentially available for interaction with the antigen receptor on T cells. Pockets in the peptide-binding site accommodate five of the thirteen side chains of the bound peptide, and explain the peptide specificity of HLA-DR1. Twelve hydrogen bonds between conserved HLA-DR1 residues and the main chain of the peptide provide a universal mode of peptide binding, distinct from the strategy used by class I histocompatibility proteins.
 ==About this Structure==
 DLH is a [[Protein complex]] structure. The following page contains interesting information on the relation of 1DLH with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb62_1.html Major Histocompatibility Complex]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLH OCA].
-==Reference==
-Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide., Stern LJ, Brown JH, Jardetzky TS, Gorga JC, Urban RG, Strominger JL, Wiley DC, Nature. 1994 Mar 17;368(6468):215-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8145819 8145819]
 [[Category: Major Histocompatibility Complex]]
 [[Category: Protein complex]]
 [[Category: Stern, L J.]]
 [[Category: Histocompatibility antigen]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:59:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:11:09 2008''