1uqs

From Proteopedia

(Difference between revisions)

Revision as of 13:34, 6 January 2015

THE CRYSTAL STRUCTURE OF HUMAN CD1B WITH A BOUND BACTERIAL GLYCOLIPID

Structural highlights

1uqs is a 2 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:
Related:	1gzp, 1gzq, 1a1m, 1a1n, 1a1o, 1a6z, 1a9b, 1a9e, 1agb, 1agc, 1agd, 1age, 1agf, 1akj, 1ao7, 1b0g, 1ce6, 1de4, 1e27, 1e28, 1eey, 1eez, 1efx, 1exu, 1hhg, 1hhh, 1hhi, 1hhj, 1hhk, 1hla, 1hsa, 1hsb, 1i4f, 1i7r, 1i7t, 1i7u, 1im3, 1im9, 1jf1, 1jgd, 1jge, 1jht, 1jnj, 1k5n, 1kpr, 1ktl, 1lds, 1m05, 1m6o, 1mi5, 1of2, 1oga, 1ogt, 1qlf, 1qqd, 1tmc, 2clr, 2hla, 3hla
Resources:	FirstGlance, OCA, RCSB, PDBsum

Disease

[B2MG_HUMAN] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:241600]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.^[1] Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10] ^[11] ^[12] ^[13] ^[14]

Function

[B2MG_HUMAN] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide 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

The human MHC class I-like molecule CD1b is distinctive among CD1 alleles in that it is capable of presenting a set of glycolipid species that show a very broad range of variation in the lengths of their acyl chains. A structure of CD1b complexed with relatively short acyl chain glycolipids plus detergent suggested how an interlinked network of channels within the Ag-binding groove could accommodate acyl chain lengths of up to 80 carbons. The structure of CD1b complexed with glucose monomycolate, reported in this study, confirms this hypothesis and illustrates how the distinctive substituents of intracellular bacterial glycolipids can be accommodated. The Ag-binding groove of CD1b is, uniquely among CD1 alleles, partitioned into channels suitable for the compact accommodation of lengthy acyl chains. The current crystal structure illustrates for the first time the binding of a natural bacterial lipid Ag to CD1b and shows how its novel structural features fit this molecule for its role in the immune response to intracellular bacteria.

The crystal structure of human CD1b with a bound bacterial glycolipid.,Batuwangala T, Shepherd D, Gadola SD, Gibson KJ, Zaccai NR, Fersht AR, Besra GS, Cerundolo V, Jones EY J Immunol. 2004 Feb 15;172(4):2382-8. PMID:14764708^[15]

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

References

↑ Wani MA, Haynes LD, Kim J, Bronson CL, Chaudhury C, Mohanty S, Waldmann TA, Robinson JM, Anderson CL. Familial hypercatabolic hypoproteinemia caused by deficiency of the neonatal Fc receptor, FcRn, due to a mutant beta2-microglobulin gene. Proc Natl Acad Sci U S A. 2006 Mar 28;103(13):5084-9. Epub 2006 Mar 20. PMID:16549777 doi:10.1073/pnas.0600548103
↑ Gorevic PD, Munoz PC, Casey TT, DiRaimondo CR, Stone WJ, Prelli FC, Rodrigues MM, Poulik MD, Frangione B. Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis. Proc Natl Acad Sci U S A. 1986 Oct;83(20):7908-12. PMID:3532124
↑ Argiles A, Derancourt J, Jauregui-Adell J, Mion C, Demaille JG. Biochemical characterization of serum and urinary beta 2 microglobulin in end-stage renal disease patients. Nephrol Dial Transplant. 1992;7(11):1106-10. PMID:1336137
↑ Momoi T, Suzuki M, Titani K, Hisanaga S, Ogawa H, Saito A. Amino acid sequence of a modified beta 2-microglobulin in renal failure patient urine and long-term dialysis patient blood. Clin Chim Acta. 1995 May 15;236(2):135-44. PMID:7554280
↑ Cunningham BA, Wang JL, Berggard I, Peterson PA. The complete amino acid sequence of beta 2-microglobulin. Biochemistry. 1973 Nov 20;12(24):4811-22. PMID:4586824
↑ Haag-Weber M, Mai B, Horl WH. Isolation of a granulocyte inhibitory protein from uraemic patients with homology of beta 2-microglobulin. Nephrol Dial Transplant. 1994;9(4):382-8. PMID:8084451
↑ Trinh CH, Smith DP, Kalverda AP, Phillips SE, Radford SE. Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties. Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9771-6. Epub 2002 Jul 15. PMID:12119416 doi:10.1073/pnas.152337399
↑ Stewart-Jones GB, McMichael AJ, Bell JI, Stuart DI, Jones EY. A structural basis for immunodominant human T cell receptor recognition. Nat Immunol. 2003 Jul;4(7):657-63. Epub 2003 Jun 8. PMID:12796775 doi:10.1038/ni942
↑ Kihara M, Chatani E, Iwata K, Yamamoto K, Matsuura T, Nakagawa A, Naiki H, Goto Y. Conformation of amyloid fibrils of beta2-microglobulin probed by tryptophan mutagenesis. J Biol Chem. 2006 Oct 13;281(41):31061-9. Epub 2006 Aug 10. PMID:16901902 doi:10.1074/jbc.M605358200
↑ Eakin CM, Berman AJ, Miranker AD. A native to amyloidogenic transition regulated by a backbone trigger. Nat Struct Mol Biol. 2006 Mar;13(3):202-8. Epub 2006 Feb 19. PMID:16491088 doi:10.1038/nsmb1068
↑ Iwata K, Matsuura T, Sakurai K, Nakagawa A, Goto Y. High-resolution crystal structure of beta2-microglobulin formed at pH 7.0. J Biochem. 2007 Sep;142(3):413-9. Epub 2007 Jul 23. PMID:17646174 doi:10.1093/jb/mvm148
↑ Ricagno S, Colombo M, de Rosa M, Sangiovanni E, Giorgetti S, Raimondi S, Bellotti V, Bolognesi M. DE loop mutations affect beta2-microglobulin stability and amyloid aggregation. Biochem Biophys Res Commun. 2008 Dec 5;377(1):146-50. Epub 2008 Oct 1. PMID:18835253 doi:S0006-291X(08)01866-4
↑ 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
↑ Ricagno S, Raimondi S, Giorgetti S, Bellotti V, Bolognesi M. Human beta-2 microglobulin W60V mutant structure: Implications for stability and amyloid aggregation. Biochem Biophys Res Commun. 2009 Mar 13;380(3):543-7. Epub 2009 Jan 25. PMID:19284997 doi:10.1016/j.bbrc.2009.01.116
↑ Batuwangala T, Shepherd D, Gadola SD, Gibson KJ, Zaccai NR, Fersht AR, Besra GS, Cerundolo V, Jones EY. The crystal structure of human CD1b with a bound bacterial glycolipid. J Immunol. 2004 Feb 15;172(4):2382-8. PMID:14764708

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uqs"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1uqs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UQS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UQS FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GMM:GLUCOSE+MONOMYCOLATE'>GMM</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GMM:GLUCOSE+MONOMYCOLATE'>GMM</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gzp|1gzp]], [[1gzq|1gzq]], [[1a1m|1a1m]], [[1a1n|1a1n]], [[1a1o|1a1o]], [[1a6z|1a6z]], [[1a9b|1a9b]], [[1a9e|1a9e]], [[1agb|1agb]], [[1agc|1agc]], [[1agd|1agd]], [[1age|1age]], [[1agf|1agf]], [[1akj|1akj]], [[1ao7|1ao7]], [[1b0g|1b0g]], [[1ce6|1ce6]], [[1de4|1de4]], [[1e27|1e27]], [[1e28|1e28]], [[1eey|1eey]], [[1eez|1eez]], [[1efx|1efx]], [[1exu|1exu]], [[1hhg|1hhg]], [[1hhh|1hhh]], [[1hhi|1hhi]], [[1hhj|1hhj]], [[1hhk|1hhk]], [[1hla|1hla]], [[1hsa|1hsa]], [[1hsb|1hsb]], [[1i4f|1i4f]], [[1i7r|1i7r]], [[1i7t|1i7t]], [[1i7u|1i7u]], [[1im3|1im3]], [[1im9|1im9]], [[1jf1|1jf1]], [[1jgd|1jgd]], [[1jge|1jge]], [[1jht|1jht]], [[1jnj|1jnj]], [[1k5n|1k5n]], [[1kpr|1kpr]], [[1ktl|1ktl]], [[1lds|1lds]], [[1m05|1m05]], [[1m6o|1m6o]], [[1mi5|1mi5]], [[1of2|1of2]], [[1oga|1oga]], [[1ogt|1ogt]], [[1qlf|1qlf]], [[1qqd|1qqd]], [[1tmc|1tmc]], [[2clr|2clr]], [[2hla|2hla]], [[3hla|3hla]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gzp|1gzp]], [[1gzq|1gzq]], [[1a1m|1a1m]], [[1a1n|1a1n]], [[1a1o|1a1o]], [[1a6z|1a6z]], [[1a9b|1a9b]], [[1a9e|1a9e]], [[1agb|1agb]], [[1agc|1agc]], [[1agd|1agd]], [[1age|1age]], [[1agf|1agf]], [[1akj|1akj]], [[1ao7|1ao7]], [[1b0g|1b0g]], [[1ce6|1ce6]], [[1de4|1de4]], [[1e27|1e27]], [[1e28|1e28]], [[1eey|1eey]], [[1eez|1eez]], [[1efx|1efx]], [[1exu|1exu]], [[1hhg|1hhg]], [[1hhh|1hhh]], [[1hhi|1hhi]], [[1hhj|1hhj]], [[1hhk|1hhk]], [[1hla|1hla]], [[1hsa|1hsa]], [[1hsb|1hsb]], [[1i4f|1i4f]], [[1i7r|1i7r]], [[1i7t|1i7t]], [[1i7u|1i7u]], [[1im3|1im3]], [[1im9|1im9]], [[1jf1|1jf1]], [[1jgd|1jgd]], [[1jge|1jge]], [[1jht|1jht]], [[1jnj|1jnj]], [[1k5n|1k5n]], [[1kpr|1kpr]], [[1ktl|1ktl]], [[1lds|1lds]], [[1m05|1m05]], [[1m6o|1m6o]], [[1mi5|1mi5]], [[1of2|1of2]], [[1oga|1oga]], [[1ogt|1ogt]], [[1qlf|1qlf]], [[1qqd|1qqd]], [[1tmc|1tmc]], [[2clr|2clr]], [[2hla|2hla]], [[3hla|3hla]]</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uqs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1uqs RCSB], [http://www.ebi.ac.uk/pdbsum/1uqs 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=1uqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uqs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1uqs RCSB], [http://www.ebi.ac.uk/pdbsum/1uqs PDBsum]</span></td></tr>
-<table>
+</table>
 == Disease ==
 [[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Defects in B2M are the cause of hypercatabolic hypoproteinemia (HYCATHYP) [MIM:[http://omim.org/entry/241600 241600]]. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation.<ref>PMID:16549777</ref>   Note=Beta-2-microglobulin may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. Persistently high beta(2)-microglobulin serum levels lead to amyloidosis in patients on long-term hemodialysis.<ref>PMID:3532124</ref> <ref>PMID:1336137</ref> <ref>PMID:7554280</ref> <ref>PMID:4586824</ref> <ref>PMID:8084451</ref> <ref>PMID:12119416</ref> <ref>PMID:12796775</ref> <ref>PMID:16901902</ref> <ref>PMID:16491088</ref> <ref>PMID:17646174</ref> <ref>PMID:18835253</ref> <ref>PMID:18395224</ref> <ref>PMID:19284997</ref>
@@ Line 37: / Line 37: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Batuwangala, T.]]
+[[Category: Batuwangala, T]]
-[[Category: Besra, G S.]]
+[[Category: Besra, G S]]
-[[Category: Cerundolo, V.]]
+[[Category: Cerundolo, V]]
-[[Category: Gadola, S D.]]
+[[Category: Gadola, S D]]
-[[Category: Gibson, K J.C.]]
+[[Category: Gibson, K J.C]]
-[[Category: Jones, E Y.]]
+[[Category: Jones, E Y]]
-[[Category: Shepherd, D.]]
+[[Category: Shepherd, D]]
-[[Category: Zaccai, N R.]]
+[[Category: Zaccai, N R]]
 [[Category: Antigen presentation]]
 [[Category: Cd1b]]

1uqs

From Proteopedia

Revision as of 13:34, 6 January 2015

THE CRYSTAL STRUCTURE OF HUMAN CD1B WITH A BOUND BACTERIAL GLYCOLIPID

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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