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2vb5

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Revision as of 17:47, 8 February 2016

SOLUTION STRUCTURE OF W60G MUTANT OF HUMAN BETA2-MICROGLOBULIN

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

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties. J Mol Biol. 2008 May 9;378(4):887-97. Epub 2008 Mar 8. PMID:18395224 doi:10.1016/j.jmb.2008.03.002

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vb5"

@@ Line 2: / Line 2: @@
 <StructureSection load='2vb5' size='340' side='right' caption='[[2vb5]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vb5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VB5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VB5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vb5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VB5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VB5 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a1m|1a1m]], [[1a6z|1a6z]], [[1agd|1agd]], [[1akj|1akj]], [[1ce6|1ce6]], [[1cg9|1cg9]], [[1duy|1duy]], [[1duz|1duz]], [[1e27|1e27]], [[1eez|1eez]], [[1efx|1efx]], [[1exu|1exu]], [[1gzq|1gzq]], [[1hla|1hla]], [[1hsa|1hsa]], [[1hsb|1hsb]], [[1i7r|1i7r]], [[1im3|1im3]], [[1jgd|1jgd]], [[1k5n|1k5n]], [[1ktl|1ktl]], [[1lp9|1lp9]], [[1m6o|1m6o]], [[1a1n|1a1n]], [[1a1o|1a1o]], [[1a9b|1a9b]], [[1a9e|1a9e]], [[1agb|1agb]], [[1agc|1agc]], [[1age|1age]], [[1agf|1agf]], [[1ao7|1ao7]], [[1b0g|1b0g]], [[1b0r|1b0r]], [[1bd2|1bd2]], [[1c16|1c16]], [[1de4|1de4]], [[1e28|1e28]], [[1eey|1eey]], [[1gzp|1gzp]], [[1hhg|1hhg]], [[1hhh|1hhh]], [[1hhi|1hhi]], [[1mi5|1mi5]], [[1n2r|1n2r]], [[1of2|1of2]], [[1oga|1oga]], [[1ogt|1ogt]], [[1onq|1onq]], [[1q94|1q94]], [[1qew|1qew]], [[1qqd|1qqd]], [[1qrn|1qrn]], [[1qsf|1qsf]], [[1s9w|1s9w]], [[1s9x|1s9x]], [[1s9y|1s9y]], [[1syv|1syv]], [[1tvh|1tvh]], [[1uqs|1uqs]], [[1ur7|1ur7]], [[1uxw|1uxw]], [[1hhj|1hhj]], [[1hhk|1hhk]], [[1i1f|1i1f]], [[1i1y|1i1y]], [[1i4f|1i4f]], [[1i7t|1i7t]], [[1i7u|1i7u]], [[1im9|1im9]], [[1jf1|1jf1]], [[1jge|1jge]], [[1jht|1jht]], [[1jnj|1jnj]], [[1kpr|1kpr]], [[1lds|1lds]], [[1m05|1m05]], [[1mhe|1mhe]], [[1p7q|1p7q]], [[1py4|1py4]], [[1qlf|1qlf]], [[1qr1|1qr1]], [[1qse|1qse]], [[1qvo|1qvo]], [[1r3h|1r3h]], [[1sys|1sys]], [[1x7q|1x7q]], [[1xh3|1xh3]], [[1xr8|1xr8]], [[1ydp|1ydp]], [[1ypz|1ypz]], [[2a83|2a83]], [[2av7|2av7]], [[2axg|2axg]], [[2bnq|2bnq]], [[2bnr|2bnr]], [[2bsr|2bsr]], [[2bsu|2bsu]], [[2c7u|2c7u]], [[2cii|2cii]], [[2d31|2d31]], [[2esv|2esv]], [[2h26|2h26]], [[2uwe|2uwe]], [[2v2x|2v2x]], [[1tmc|1tmc]], [[1tvb|1tvb]], [[1uxs|1uxs]], [[1vgk|1vgk]], [[1w0v|1w0v]], [[1w0w|1w0w]], [[1w72|1w72]], [[1xr9|1xr9]], [[1xz0|1xz0]], [[1zs8|1zs8]], [[1zsd|1zsd]], [[1zt4|1zt4]], [[2ak4|2ak4]], [[2axf|2axf]], [[2bck|2bck]], [[2bss|2bss]], [[2bst|2bst]], [[2bsv|2bsv]], [[2bvq|2bvq]], [[2cik|2cik]], [[2clr|2clr]], [[2f74|2f74]], [[2f8o|2f8o]], [[2hjk|2hjk]], [[2hjl|2hjl]], [[2hla|2hla]], [[2jcc|2jcc]], [[2v2w|2v2w]], [[3hla|3hla]], [[1bmg|1bmg]], [[2e8d|2e8d]], [[2d4d|2d4d]], [[2d4f|2d4f]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vb5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vb5 RCSB], [http://www.ebi.ac.uk/pdbsum/2vb5 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vb5 OCA], [http://pdbe.org/2vb5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vb5 RCSB], [http://www.ebi.ac.uk/pdbsum/2vb5 PDBsum]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 14: / Line 14: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vb5 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 24: / Line 24: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2vb5" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Bellotti, V]]
 [[Category: Bolognesi, B]]

2vb5

From Proteopedia

Revision as of 17:47, 8 February 2016

SOLUTION STRUCTURE OF W60G MUTANT OF HUMAN BETA2-MICROGLOBULIN

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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