1ktd

<table><tr><td colspan='2'>[[1ktd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Colli Colli] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1KTD FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kt2|1kt2]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H2-Ea ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), H2-Eb1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8932 COLLI])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ktd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ktd OCA], [http://pdbe.org/1ktd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ktd RCSB], [http://www.ebi.ac.uk/pdbsum/1ktd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ktd ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CYC_COLLI CYC_COLLI]] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.

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== Publication Abstract from PubMed ==

The COOH-terminal peptides of pigeon and moth cytochrome c, bound to mouse IE(k), are two of the most thoroughly studied T cell antigens. We have solved the crystal structures of the moth peptide and a weak agonist-antagonist variant of the pigeon peptide bound to IE(k). The moth peptide and all other peptides whose structures have been solved bound to IE(k), have a lysine filling the p9 pocket of IE(k). However, the pigeon peptide has an alanine at p9 shifting the lysine to p10. Rather than kinking to place the lysine in the anchor pocket, the pigeon peptide takes the extended course through the binding groove, which is characteristic of all other peptides bound to major histocompatibility complex (MHC) class II. Thus, unlike MHC class I, in which peptides often kink to place optimally anchoring side chains, MHC class II imposes an extended peptide conformation even at the cost of a highly conserved anchor residue. The substitution of Ser for Thr at p8 in the variant pigeon peptide induces no detectable surface change other than the loss of the side chain methyl group, despite the dramatic change in recognition by T cells. Finally, these structures can be used to interpret the many published mutational studies of these ligands and the T cell receptors that recognize them.

Structural basis of cytochrome c presentation by IE(k).,Fremont DH, Dai S, Chiang H, Crawford F, Marrack P, Kappler J J Exp Med. 2002 Apr 15;195(8):1043-52. PMID:11956295<ref>PMID:11956295</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ktd" style="background-color:#fffaf0;"></div>

[[Category: Colli]]

[[Category: Lk3 transgenic mice]]

[[Category: Chiang, H]]

[[Category: Crawford, F]]

[[Category: Dai, S]]

[[Category: Fremont, D H]]

[[Category: Kappler, J]]

[[Category: Marrack, P]]

[[Category: T cell receptor]]