1fo0: Difference between revisions

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[[Image:1fo0.gif|left|200px]]<br /><applet load="1fo0" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1fo0.gif|left|200px]]<br /><applet load="1fo0" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1fo0, resolution 2.50Å" />

'''MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE COMPLEX'''<br />

==Overview==

Many T cell receptors (TCRs) that are selected to respond to foreign, peptide antigens bound to self major histocompatibility complex (MHC), molecules are also reactive with allelic variants of self-MHC molecules., This property, termed alloreactivity, causes graft rejection and, graft-versus-host disease. The structural features of alloreactivity have, yet to be defined. We now present a basis for this cross-reactivity, elucidated by the crystal structure of a complex involving the BM3.3 TCR, and a naturally processed octapeptide bound to the H-2Kb allogeneic MHC, class I molecule. A distinguishing feature of this complex is that the, eleven-residue-long complementarity-determining region 3 (CDR3) found in, the BM3.3 TCR alpha chain folds away from the peptide binding groove and, makes no contact with the bound peptide, the latter being exclusively, contacted by the BM3.3 CDR3 beta. Our results formally establish that, peptide-specific, alloreactive TCRs interact with allo-MHC in a register, similar to the one they use to contact self-MHC molecules.

Many T cell receptors (TCRs) that are selected to respond to foreign peptide antigens bound to self major histocompatibility complex (MHC) molecules are also reactive with allelic variants of self-MHC molecules. This property, termed alloreactivity, causes graft rejection and graft-versus-host disease. The structural features of alloreactivity have yet to be defined. We now present a basis for this cross-reactivity, elucidated by the crystal structure of a complex involving the BM3.3 TCR and a naturally processed octapeptide bound to the H-2Kb allogeneic MHC class I molecule. A distinguishing feature of this complex is that the eleven-residue-long complementarity-determining region 3 (CDR3) found in the BM3.3 TCR alpha chain folds away from the peptide binding groove and makes no contact with the bound peptide, the latter being exclusively contacted by the BM3.3 CDR3 beta. Our results formally establish that peptide-specific, alloreactive TCRs interact with allo-MHC in a register similar to the one they use to contact self-MHC molecules.

==About this Structure==

1FO0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1FO0 OCA].

1FO0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FO0 OCA].

==Reference==

Line 14:

[[Category: Protein complex]]

[[Category: Darnault, C.]]

[[Category: Fontecilla-Camps, J.C.]]

[[Category: Fontecilla-Camps, J C.]]

[[Category: Gregoire, C.]]

[[Category: Guimezanes, A.]]

Line 21:

[[Category: Mazza, G.]]

[[Category: Mosser, T.]]

[[Category: Reiser, J.B.]]

[[Category: Reiser, J B.]]

[[Category: Schmitt-Verhulst, A-M.]]

[[Category: class i mhc]]

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[[Category: tcr-pmhc complex]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:43 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1fo0.gif|left|200px]]<br /><applet load="1fo0" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fo0.gif|left|200px]]<br /><applet load="1fo0" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fo0, resolution 2.50&Aring;" />
 '''MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE COMPLEX'''<br />
 ==Overview==
-Many T cell receptors (TCRs) that are selected to respond to foreign, peptide antigens bound to self major histocompatibility complex (MHC), molecules are also reactive with allelic variants of self-MHC molecules., This property, termed alloreactivity, causes graft rejection and, graft-versus-host disease. The structural features of alloreactivity have, yet to be defined. We now present a basis for this cross-reactivity, elucidated by the crystal structure of a complex involving the BM3.3 TCR, and a naturally processed octapeptide bound to the H-2Kb allogeneic MHC, class I molecule. A distinguishing feature of this complex is that the, eleven-residue-long complementarity-determining region 3 (CDR3) found in, the BM3.3 TCR alpha chain folds away from the peptide binding groove and, makes no contact with the bound peptide, the latter being exclusively, contacted by the BM3.3 CDR3 beta. Our results formally establish that, peptide-specific, alloreactive TCRs interact with allo-MHC in a register, similar to the one they use to contact self-MHC molecules.
+Many T cell receptors (TCRs) that are selected to respond to foreign peptide antigens bound to self major histocompatibility complex (MHC) molecules are also reactive with allelic variants of self-MHC molecules. This property, termed alloreactivity, causes graft rejection and graft-versus-host disease. The structural features of alloreactivity have yet to be defined. We now present a basis for this cross-reactivity, elucidated by the crystal structure of a complex involving the BM3.3 TCR and a naturally processed octapeptide bound to the H-2Kb allogeneic MHC class I molecule. A distinguishing feature of this complex is that the eleven-residue-long complementarity-determining region 3 (CDR3) found in the BM3.3 TCR alpha chain folds away from the peptide binding groove and makes no contact with the bound peptide, the latter being exclusively contacted by the BM3.3 CDR3 beta. Our results formally establish that peptide-specific, alloreactive TCRs interact with allo-MHC in a register similar to the one they use to contact self-MHC molecules.
 ==About this Structure==
-FO0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FO0 OCA].
+FO0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FO0 OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Protein complex]]
 [[Category: Darnault, C.]]
-[[Category: Fontecilla-Camps, J.C.]]
+[[Category: Fontecilla-Camps, J C.]]
 [[Category: Gregoire, C.]]
 [[Category: Guimezanes, A.]]
@@ Line 21: / Line 21: @@
 [[Category: Mazza, G.]]
 [[Category: Mosser, T.]]
-[[Category: Reiser, J.B.]]
+[[Category: Reiser, J B.]]
 [[Category: Schmitt-Verhulst, A-M.]]
 [[Category: class i mhc]]
@@ Line 28: / Line 28: @@
 [[Category: tcr-pmhc complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:04:55 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:43 2008''