1g7p: Difference between revisions

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|PDB= 1g7p |SIZE=350|CAPTION= <scene name='initialview01'>1g7p</scene>, resolution 1.50&Aring;
|PDB= 1g7p |SIZE=350|CAPTION= <scene name='initialview01'>1g7p</scene>, resolution 1.50&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
|LIGAND= <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
|ACTIVITY= [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]  
|ACTIVITY= <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>
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[2vab|2VAB]], [[1vad|1VAD]]
|RESOURCES=<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.ebi.ac.uk/pdbsum/1g7p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g7p RCSB]</span>
}}
}}


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[[Category: Wilson, I A.]]
[[Category: Wilson, I A.]]
[[Category: Yu, M.]]
[[Category: Yu, M.]]
[[Category: NAG]]
[[Category: alpha-glucosidase]]
[[Category: alpha-glucosidase]]
[[Category: h-2kb]]
[[Category: h-2kb]]
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[[Category: yeast]]
[[Category: yeast]]


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Revision as of 20:38, 30 March 2008

File:1g7p.gif


PDB ID 1g7p

Drag the structure with the mouse to rotate
, resolution 1.50Å
Ligands: ,
Activity: Alpha-glucosidase, with EC number 3.2.1.20
Related: 2VAB, 1VAD


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF MHC CLASS I H-2KB HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND YEAST ALPHA-GLUCOSIDASE


OverviewOverview

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.

About this StructureAbout this Structure

1G7P is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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

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