1g7p

<StructureSection load='1g7p' size='340' side='right' caption='[[1g7p]], [[Resolution|resolution]] 1.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[1g7p]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G7P FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene><br>

<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vab|2vab]], [[1vad|1vad]]</td></tr>

<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </span></td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g7p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g7p RCSB], [http://www.ebi.ac.uk/pdbsum/1g7p PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g7/1g7p_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The crystal structure of a non-standard peptide, YEA9, in complex with H-2Kb, at 1.5 A resolution demonstrates how YEA9 peptide can bind with surprisingly high affinity through insertion of alternative, long, non-canonical anchors into the B and E pockets. The use of "alternative pockets" represents a new mode of high affinity peptide binding, that should be considered when predicting peptide epitopes for MHC class I. These novel interactions encountered in this non-canonical high affinity peptide-MHC complex should help predict additional binding peptides from primary protein sequences and aid in the design of alternative approaches for peptide-based vaccines.

Crystal structure of a non-canonical high affinity peptide complexed with MHC class I: a novel use of alternative anchors.,Apostolopoulos V, Yu M, Corper AL, Li W, McKenzie IF, Teyton L, Wilson IA, Plebanski M J Mol Biol. 2002 May 17;318(5):1307-16. PMID:12083519<ref>PMID:12083519</ref>

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

</div>

*[[Beta-2 microglobulin|Beta-2 microglobulin]]

*[[Major histocompatibility complex|Major histocompatibility complex]]

[[Category: Alpha-glucosidase]]

[[Category: Apostolopoulos, V.]]

[[Category: Corper, A L.]]

[[Category: Li, W.]]

[[Category: McKenzie, I F.]]

[[Category: Teyton, L.]]

[[Category: Wilson, I A.]]

[[Category: Yu, M.]]

[[Category: Yeast]]