2x4s | pdb_00002x4s

CRYSTAL STRUCTURE OF MHC CLASS I HLA-A2.1 BOUND TO A PEPTIDE REPRESENTING THE EPITOPE OF THE H5N1 (AVIAN FLU) NUCLEOPROTEIN

spinqualitylabelsall models 2x4s, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2x4s is a 6 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, MES NonStd Res: MSE Related: 1uqs, 1bd2, 2esv, 2ak4, 1ypz, 1im3, 1uxw, 1i7u, 1c16, 1hsa, 1gzp, 2axf, 2bnq, 1w72, 2jcc, 2bck, 1de4, 2vlk, 1exu, 1qrn, 2hla, 1mhe, 1im9, 1eez, 1jht, 1qqd, 1qr1, 1zs8, 1hla, 1jgd, 1i1y, 1vgk, 1age, 1ur7, 1hhg, 1s9x, 1a9e, 1duz, 2clr, 3hla, 1m05, 1tvb, 2v2w, 1onq, 2vlr, 1a1n, 2bvo, 1lp9, 1zsd, 1m6o, 1hhk, 1hsb, 1zt4, 1x7q, 1ce6, 1py4, 1syv, 2j8u, 1sys, 1ogt, 1cg9, 1p7q, 1q94, 1jnj, 1agb, 2d31, 1aqd, 1xz0, 1lds, 1tvh, 1hhh, 1xr8, 2bss, 1e28, 1a1m, 2bvp, 2v2x, 1xr9, 2gj6, 1qlf, 1efx, 2av1, 1tmc, 1qsf, 1duy, 1kpr, 1jge, 2hjl, 1qew, 1w0v, 1k5n, 1ao7, 2bnr, 1xh3, 2bst, 1mi5, 2h26, 1s9y, 1a1o, 2a83, 1agf, 1oga, 2f8o, 2cii, 1i7r, 1jf1, 2c7u, 1e27, 2f74, 1w0w, 1gzq, 1uxs, 1akj, 2hjk, 2vb5, 1agd, 1r3h, 1eey, 1i7t, 1i4f, 1ydp, 2vll, 2bsr, 2vlj, 1b0r, 1b0g, 1of2, 1hhi, 1qse, 2axg, 1a9b, 2bvq, 1agc, 1hhj, 1qvo, 1s9w, 1ktl, 1a6z, 2cik, 2uwe, 1i1f, 2av7, 2x4r, 2x4o, 2x4u, 2x4p, 2x4q, 2x4t, 2x4n Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [1A02_HUMAN] Involved in the presentation of foreign antigens to the immune system. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed High-throughput structure determination of protein-ligand complexes is central in drug development and structural proteomics. To facilitate such high-throughput structure determination we designed an induced replacement strategy. Crystals of a protein complex bound to a photosensitive ligand are exposed to UV light, inducing the departure of the bound ligand, allowing a new ligand to soak in. We exemplify the approach for a class of protein complexes that is especially recalcitrant to high-throughput strategies: the MHC class I proteins. We developed a UV-sensitive, "conditional", peptide ligand whose UV-induced cleavage in the crystals leads to the exchange of the low-affinity lytic fragments for full-length peptides introduced in the crystallant solution. This "in crystallo" exchange is monitored by the loss of seleno-methionine anomalous diffraction signal of the conditional peptide compared to the signal of labeled MHC beta2m subunit. This method has the potential to facilitate high-throughput crystallography in various protein families. UV-induced ligand exchange in MHC class I protein crystals.,Celie PH, Toebes M, Rodenko B, Ovaa H, Perrakis A, Schumacher TN J Am Chem Soc. 2009 Sep 2;131(34):12298-304. PMID:19655750 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-2 microglobulin Major histocompatibility complex

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