1ed3: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
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...
 
No edit summary
Line 1: Line 1:
[[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==
Line 13: Line 13:
[[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]]
Line 27: Line 27:
[[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''

Revision as of 13:26, 21 February 2008

File:1ed3.gif


1ed3, resolution 2.55Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF RAT MINOR HISTOCOMPATIBILITY ANTIGEN COMPLEX RT1-AA/MTF-E.

OverviewOverview

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 StructureAbout this Structure

1ED3 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Two different, highly exposed, bulged structures for an unusually long peptide bound to rat MHC class I RT1-Aa., Speir JA, Stevens J, Joly E, Butcher GW, Wilson IA, Immunity. 2001 Jan;14(1):81-92. PMID:11163232

Page seeded by OCA on Thu Feb 21 12:26:31 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA