| Structural highlights
2x4n is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | ,
| | NonStd Res: | , |
| Related: | 1uqs, 1bd2, 2esv, 2ak4, 1ypz, 1im3, 1uxw, 1i7u, 1c16, 1hsa, 2axf, 1gzp, 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, 2x4u, 2clr, 3hla, 1m05, 2x4o, 1tvb, 2v2w, 1onq, 2vlr, 2x4p, 2bvo, 1a1n, 1lp9, 1zsd, 1m6o, 1hhk, 1hsb, 1zt4, 1ce6, 1x7q, 1py4, 1syv, 2j8u, 1sys, 1ogt, 2x4t, 1cg9, 1p7q, 1q94, 1jnj, 1agb, 2d31, 1aqd, 1xz0, 1lds, 1tvh, 1hhh, 1xr8, 2bss, 1e28, 1a1m, 2bvp, 2v2x, 1xr9, 2gj6, 2x4r, 1efx, 1qlf, 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, 2f74, 1e27, 1w0w, 1gzq, 1uxs, 1akj, 2hjk, 2vb5, 1agd, 1r3h, 1eey, 1i7t, 1ydp, 1i4f, 2vll, 2bsr, 1of2, 2vlj, 2x4s, 1b0r, 1b0g, 1hhi, 1qse, 2axg, 1a9b, 2bvq, 1agc, 1qvo, 1hhj, 1s9w, 1ktl, 1a6z, 2cik, 2uwe, 1i1f, 2av7 |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Celie PH, Toebes M, Rodenko B, Ovaa H, Perrakis A, Schumacher TN. UV-induced ligand exchange in MHC class I protein crystals. J Am Chem Soc. 2009 Sep 2;131(34):12298-304. PMID:19655750 doi:10.1021/ja9037559
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