1sbb: Difference between revisions
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<StructureSection load='1sbb' size='340' side='right'caption='[[1sbb]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1sbb' size='340' side='right'caption='[[1sbb]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1sbb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1sbb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SBB FirstGlance]. <br> | ||
</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=1sbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sbb OCA], [https://pdbe.org/1sbb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sbb RCSB], [https://www.ebi.ac.uk/pdbsum/1sbb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sbb 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]] 2.4Å</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=1sbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sbb OCA], [https://pdbe.org/1sbb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sbb RCSB], [https://www.ebi.ac.uk/pdbsum/1sbb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sbb ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/TCB1_MOUSE TCB1_MOUSE] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: | [[Category: Staphylococcus aureus]] | ||
[[Category: | [[Category: Li H]] | ||
[[Category: | [[Category: Mariuzza RA]] | ||
Revision as of 09:15, 23 August 2023
T-CELL RECEPTOR BETA CHAIN COMPLEXED WITH SUPERANTIGEN SEBT-CELL RECEPTOR BETA CHAIN COMPLEXED WITH SUPERANTIGEN SEB
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSuperantigens (SAGs) are a class of immunostimulatory proteins of bacterial or viral origin that activate T cells by binding to the V beta domain of the T cell antigen receptor (TCR). The three-dimensional structure of the complex between a TCR beta chain (mouse V beta8.2) and the SAG staphylococcal enterotoxin B (SEB) at 2.4 A resolution reveals why SEB recognizes only certain V beta families, as well as why only certain SAGs bind mouse V beta8.2. Models of the TCR-SEB-peptide/MHC class II complex indicate that V alpha interacts with the MHC beta chain in the TCR-SAG-MHC complex. The extent of the interaction is variable and is largely determined by the geometry of V alpha/V beta domain association. This variability can account for the preferential expression of certain V alpha regions among T cells reactive with SEB. Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B.,Li H, Llera A, Tsuchiya D, Leder L, Ysern X, Schlievert PM, Karjalainen K, Mariuzza RA Immunity. 1998 Dec;9(6):807-16. PMID:9881971[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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