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New page: left|200px<br /><applet load="1ed3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ed3, resolution 2.55Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1ed3.gif|left|200px]]<br /><applet load="1ed3" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ed3.gif|left|200px]]<br /><applet load="1ed3" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ed3, resolution 2.55&Aring;" />
caption="1ed3, resolution 2.55&Aring;" />
'''CRYSTAL STRUCTURE OF RAT MINOR HISTOCOMPATIBILITY ANTIGEN COMPLEX RT1-AA/MTF-E.'''<br />
'''CRYSTAL STRUCTURE OF RAT MINOR HISTOCOMPATIBILITY ANTIGEN COMPLEX RT1-AA/MTF-E.'''<br />


==Overview==
==Overview==
The rat MHC class Ia molecule RT1-Aa has the unusual capacity to bind long, peptides ending in arginine, such as MTF-E, a thirteen-residue, maternally, transmitted minor histocompatibility antigen. The antigenic structure of, MTF-E was unpredictable due to its extraordinary length and two arginines, that could serve as potential anchor residues. The crystal structure of, RT1-Aa-MTF-E at 2.55 A shows that both peptide termini are anchored, as in, other class I molecules, but the central residues in two independent pMHC, complexes adopt completely different bulged conformations based on local, environment. The MTF-E epitope is fully exposed within the putative T cell, receptor (TCR) footprint. The flexibility demonstrated by the MTF-E, structures illustrates how different TCRs may be raised against chemically, identical, but structurally dissimilar, pMHC complexes.
The rat MHC class Ia molecule RT1-Aa has the unusual capacity to bind long peptides ending in arginine, such as MTF-E, a thirteen-residue, maternally transmitted minor histocompatibility antigen. The antigenic structure of MTF-E was unpredictable due to its extraordinary length and two arginines that could serve as potential anchor residues. The crystal structure of RT1-Aa-MTF-E at 2.55 A shows that both peptide termini are anchored, as in other class I molecules, but the central residues in two independent pMHC complexes adopt completely different bulged conformations based on local environment. The MTF-E epitope is fully exposed within the putative T cell receptor (TCR) footprint. The flexibility demonstrated by the MTF-E structures illustrates how different TCRs may be raised against chemically identical, but structurally dissimilar, pMHC complexes.


==About this Structure==
==About this Structure==
1ED3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ED3 OCA].  
1ED3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ED3 OCA].  


==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Butcher, G.W.]]
[[Category: Butcher, G W.]]
[[Category: Joly, E.]]
[[Category: Joly, E.]]
[[Category: Speir, J.A.]]
[[Category: Speir, J A.]]
[[Category: Stevens, J.]]
[[Category: Stevens, J.]]
[[Category: Wilson, I.A.]]
[[Category: Wilson, I A.]]
[[Category: cell surface receptor]]
[[Category: cell surface receptor]]
[[Category: cellular immunity]]
[[Category: cellular immunity]]
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[[Category: t cell receptor ligand]]
[[Category: t cell receptor ligand]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:54:27 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:31 2008''