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1ed3

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

Structural highlights

1ed3 is a 6 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.55Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HA12_RAT Involved in the presentation of foreign antigens to the immune system.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ed3"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF RAT MINOR HISTOCOMPATIBILITY ANTIGEN COMPLEX RT1-AA/MTF-E.==
-<StructureSection load='1ed3' size='340' side='right' caption='[[1ed3]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
+<StructureSection load='1ed3' size='340' side='right'caption='[[1ed3]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ed3]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ED3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ED3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ed3]] is a 6 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ED3 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ed3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ed3 OCA], [http://pdbe.org/1ed3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ed3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ed3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ed3 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ed3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ed3 OCA], [https://pdbe.org/1ed3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ed3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ed3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ed3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HA12_RAT HA12_RAT]] Involved in the presentation of foreign antigens to the immune system. [[http://www.uniprot.org/uniprot/ATP6_RAT ATP6_RAT]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane. [[http://www.uniprot.org/uniprot/B2MG_RAT B2MG_RAT]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
+[https://www.uniprot.org/uniprot/HA12_RAT HA12_RAT] Involved in the presentation of foreign antigens to the immune system.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/1ed3_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/1ed3_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 30: @@
 ==See Also==
-*[[Beta-2 microglobulin|Beta-2 microglobulin]]
+*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
-*[[Beta-2-microglobulin|Beta-2-microglobulin]]
+*[[MHC 3D structures|MHC 3D structures]]
-*[[Major histocompatibility complex|Major histocompatibility complex]]
+*[[MHC I 3D structures|MHC I 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Butcher, G W]]
+[[Category: Large Structures]]
-[[Category: Joly, E]]
+[[Category: Rattus norvegicus]]
-[[Category: Speir, J A]]
+[[Category: Butcher GW]]
-[[Category: Stevens, J]]
+[[Category: Joly E]]
-[[Category: Wilson, I A]]
+[[Category: Speir JA]]
-[[Category: Cell surface receptor]]
+[[Category: Stevens J]]
-[[Category: Cellular immunity]]
+[[Category: Wilson IA]]
-[[Category: Immune system]]
-[[Category: Immunology]]
-[[Category: Major histocompatibility complex]]
-[[Category: Mhc]]
-[[Category: Peptide antigen presentation]]
-[[Category: Rat minor histocompatibility complex]]
-[[Category: T cell receptor ligand]]

1ed3

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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