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2vaa, resolution 2.30Å ()
Gene:	BETA-2-MICROGLOBULIN (Mus musculus)
Domains:	IGc, MHC_I
Structural annotation: Resources: CATH : 2Vaaa01, 2Vaaa02, 2Vaab00 InterPro : Ipr007110, Ipr003006, Ipr010579, Ipr013783, Ipr001039, Ipr011162, Ipr011161, Ipr003597, Ipr015707, Ipr000448 Pfam : PF07654, PF00129, PF00945 SCOP : d2vaaa2, d2vaaa1, d2vaab_ UniProt : P01901, P01887, P11212
Functional annotation: Cellular component: integral to membrane external side of plasma membrane MHC class I protein complex membrane extracellular space integral to plasma membrane virion viral nucleocapsid ribonucleoprotein complex cytoplasm Biological process: immune response antigen processing and presentation of peptide antigen via MHC class I defense response antigen processing and presentation antigen processing and presentation of endogenous peptide antigen via MHC class I antigen processing and presentation of endogenous antigen cellular defense response Molecular function: protein binding RNA binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

MHC CLASS I H-2KB HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND VESICULAR STOMATITIS VIRUS NUCLEOPROTEIN

Overview

The x-ray structures of a murine MHC class I molecule (H-2Kb) were determined in complex with two different viral peptides, derived from the vesicular stomatitis virus nucleoprotein (52-59), VSV-8, and the Sendai virus nucleoprotein (324-332), SEV-9. The H-2Kb complexes were refined at 2.3 A for VSV-8 and 2.5 A for SEV-9. The structure of H-2Kb exhibits a high degree of similarity with human HLA class I, although the individual domains can have slightly altered dispositions. Both peptides bind in extended conformations with most of their surfaces buried in the H-2Kb binding groove. The nonamer peptide maintains the same amino- and carboxyl-terminal interactions as the octamer primarily by the insertion of a bulge in the center of an otherwise beta conformation. Most of the specific interactions are between side-chain atoms of H-2Kb and main-chain atoms of peptide. This binding scheme accounts in large part for the enormous diversity of peptide sequences that bind with high affinity to class I molecules. Small but significant conformational changes in H-2Kb are associated with peptide binding, and these synergistic movements may be an integral part of the T cell receptor recognition process.

About this Structure

2VAA is a 3 chains structure with sequences from Mus musculus and Vesicular stomatitis virus. This structure supersedes the now removed PDB entry 1vaa. The February 2005 RCSB PDB Molecule of the Month feature on Major Histocompatibility Complex by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_2. Full crystallographic information is available from OCA.

Reference

Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb., Fremont DH, Matsumura M, Stura EA, Peterson PA, Wilson IA, Science. 1992 Aug 14;257(5072):919-27. PMID:1323877

Page seeded by OCA on Mon Mar 31 05:10:18 2008