2vb5 | pdb_00002vb5

Solution structure of W60G mutant of human beta2-microglobulin

spinqualitylabelsall models 2vb5, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vb5 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1a1m, 1a6z, 1agd, 1akj, 1ce6, 1cg9, 1duy, 1duz, 1e27, 1eez, 1efx, 1exu, 1gzq, 1hla, 1hsa, 1hsb, 1i7r, 1im3, 1jgd, 1k5n, 1ktl, 1lp9, 1m6o, 1a1n, 1a1o, 1a9b, 1a9e, 1agb, 1agc, 1age, 1agf, 1ao7, 1b0g, 1b0r, 1bd2, 1c16, 1de4, 1e28, 1eey, 1gzp, 1hhg, 1hhh, 1hhi, 1mi5, 1n2r, 1of2, 1oga, 1ogt, 1onq, 1q94, 1qew, 1qqd, 1qrn, 1qsf, 1s9w, 1s9x, 1s9y, 1syv, 1tvh, 1uqs, 1ur7, 1uxw, 1hhj, 1hhk, 1i1f, 1i1y, 1i4f, 1i7t, 1i7u, 1im9, 1jf1, 1jge, 1jht, 1jnj, 1kpr, 1lds, 1m05, 1mhe, 1p7q, 1py4, 1qlf, 1qr1, 1qse, 1qvo, 1r3h, 1sys, 1x7q, 1xh3, 1xr8, 1ydp, 1ypz, 2a83, 2av7, 2axg, 2bnq, 2bnr, 2bsr, 2bsu, 2c7u, 2cii, 2d31, 2esv, 2h26, 2uwe, 2v2x, 1tmc, 1tvb, 1uxs, 1vgk, 1w0v, 1w0w, 1w72, 1xr9, 1xz0, 1zs8, 1zsd, 1zt4, 2ak4, 2axf, 2bck, 2bss, 2bst, 2bsv, 2bvq, 2cik, 2clr, 2f74, 2f8o, 2hjk, 2hjl, 2hla, 2jcc, 2v2w, 3hla, 1bmg, 2e8d, 2d4d, 2d4f Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 Amyloidosis associated to hemodialysis is caused by persistently high beta(2)-microglobulin (beta(2)m) serum levels. beta(2)m is an intrinsically amyloidogenic protein whose capacity to assemble into amyloid fibrils in vitro and in vivo is concentration dependent; no beta(2)m genetic variant is known in the human population. We investigated the roles of two evolutionary conserved Trp residues in relation to beta(2)m structure, function and folding/misfolding by means of a combined biophysical and functional approach. We show that Trp60 plays a functional role in promoting the association of beta(2)m in class I major histocompatibility complex; it is exposed to the solvent at the apex of a protein loop in order to accomplish such function. The Trp60-->Gly mutation has a threefold effect: it stabilizes beta(2)m, inhibits beta(2)m amyloidogenic propensity and weakens the interaction with the class I major histocompatibility complex heavy chain. On the contrary, Trp95 is buried in the beta(2)m core; the Trp95-->Gly mutation destabilizes the protein, which is unfolded in solution, yielding nonfibrillar beta(2)m aggregates. Trp60 and Trp95 therefore play differential and complementary roles in beta(2)m, being relevant for function (Trp60) and for maintenance of a properly folded structure (Trp95) while affecting in distinct ways the intrinsic propensity of wild-type beta(2)m towards self-aggregation into amyloid fibrils. The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties.,Esposito G, Ricagno S, Corazza A, Rennella E, Gumral D, Mimmi MC, Betto E, Pucillo CE, Fogolari F, Viglino P, Raimondi S, Giorgetti S, Bolognesi B, Merlini G, Stoppini M, Bolognesi M, Bellotti V J Mol Biol. 2008 May 9;378(4):887-97. Epub 2008 Mar 8. PMID:18395224 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-2 microglobulin 3D structures

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