1ogt: Difference between revisions

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==Overview==

The products of the human leukocyte antigen subtypes HLA-B*2705 and, HLA-B*2709 differ only in residue 116 (Asp vs. His) within the peptide, binding groove but are differentially associated with the autoimmune, disease ankylosing spondylitis (AS); HLA-B*2705 occurs in AS-patients, whereas HLA-B*2709 does not. The subtypes also generate differential T, cell repertoires as exemplified by distinct T cell responses against the, self-peptide pVIPR (RRKWRRWHL). The crystal structures described here show, that pVIPR binds in an unprecedented dual conformation only to HLA-B*2705, molecules. In one binding mode, peptide pArg5 forms a salt bridge to, Asp116, connected with drastically different interactions between peptide, and heavy chain, contrasting with the second, conventional conformation, which is exclusively found in the case of B*2709. These subtype-dependent, differences in pVIPR binding link the emergence of dissimilar T cell, repertoires in individuals with HLA-B*2705 or HLA-B*2709 to the buried, Asp116/His116 polymorphism and provide novel insights into peptide, presentation by major histocompatibility antigens.

The products of the human leukocyte antigen subtypes HLA-B*2705 and HLA-B*2709 differ only in residue 116 (Asp vs. His) within the peptide binding groove but are differentially associated with the autoimmune disease ankylosing spondylitis (AS); HLA-B*2705 occurs in AS-patients, whereas HLA-B*2709 does not. The subtypes also generate differential T cell repertoires as exemplified by distinct T cell responses against the self-peptide pVIPR (RRKWRRWHL). The crystal structures described here show that pVIPR binds in an unprecedented dual conformation only to HLA-B*2705 molecules. In one binding mode, peptide pArg5 forms a salt bridge to Asp116, connected with drastically different interactions between peptide and heavy chain, contrasting with the second, conventional conformation, which is exclusively found in the case of B*2709. These subtype-dependent differences in pVIPR binding link the emergence of dissimilar T cell repertoires in individuals with HLA-B*2705 or HLA-B*2709 to the buried Asp116/His116 polymorphism and provide novel insights into peptide presentation by major histocompatibility antigens.

==Disease==

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[[Category: Protein complex]]

[[Category: Bettosini, F.]]

[[Category: Fiorillo, M.T.]]

[[Category: Fiorillo, M T.]]

[[Category: Hulsmeyer, M.]]

[[Category: Saenger, W.]]

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[[Category: mhc (major histocompatibility complex)]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The products of the human leukocyte antigen subtypes HLA-B*2705 and, HLA-B*2709 differ only in residue 116 (Asp vs. His) within the peptide, binding groove but are differentially associated with the autoimmune, disease ankylosing spondylitis (AS); HLA-B*2705 occurs in AS-patients, whereas HLA-B*2709 does not. The subtypes also generate differential T, cell repertoires as exemplified by distinct T cell responses against the, self-peptide pVIPR (RRKWRRWHL). The crystal structures described here show, that pVIPR binds in an unprecedented dual conformation only to HLA-B*2705, molecules. In one binding mode, peptide pArg5 forms a salt bridge to, Asp116, connected with drastically different interactions between peptide, and heavy chain, contrasting with the second, conventional conformation, which is exclusively found in the case of B*2709. These subtype-dependent, differences in pVIPR binding link the emergence of dissimilar T cell, repertoires in individuals with HLA-B*2705 or HLA-B*2709 to the buried, Asp116/His116 polymorphism and provide novel insights into peptide, presentation by major histocompatibility antigens.
+The products of the human leukocyte antigen subtypes HLA-B*2705 and HLA-B*2709 differ only in residue 116 (Asp vs. His) within the peptide binding groove but are differentially associated with the autoimmune disease ankylosing spondylitis (AS); HLA-B*2705 occurs in AS-patients, whereas HLA-B*2709 does not. The subtypes also generate differential T cell repertoires as exemplified by distinct T cell responses against the self-peptide pVIPR (RRKWRRWHL). The crystal structures described here show that pVIPR binds in an unprecedented dual conformation only to HLA-B*2705 molecules. In one binding mode, peptide pArg5 forms a salt bridge to Asp116, connected with drastically different interactions between peptide and heavy chain, contrasting with the second, conventional conformation, which is exclusively found in the case of B*2709. These subtype-dependent differences in pVIPR binding link the emergence of dissimilar T cell repertoires in individuals with HLA-B*2705 or HLA-B*2709 to the buried Asp116/His116 polymorphism and provide novel insights into peptide presentation by major histocompatibility antigens.
 ==Disease==
@@ Line 17: / Line 17: @@
 [[Category: Protein complex]]
 [[Category: Bettosini, F.]]
-[[Category: Fiorillo, M.T.]]
+[[Category: Fiorillo, M T.]]
 [[Category: Hulsmeyer, M.]]
 [[Category: Saenger, W.]]
@@ Line 29: / Line 29: @@
 [[Category: mhc (major histocompatibility complex)]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:57:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:33 2008''