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Histocompatibility antigen
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PDB id
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1bmg
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Cellular component
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extracellular region
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3 terms
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Biological process
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immune response
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7 terms
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Biochemical function
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protein binding
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1 term
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DOI no:
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Proc Natl Acad Sci U S A
82:4225-4229
(1985)
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PubMed id:
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Three-dimensional structure of beta 2-microglobulin.
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J.W.Becker,
G.N.Reeke.
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ABSTRACT
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The three-dimensional structure of beta 2-microglobulin, the light chain of the
major histocompatibility complex class I antigens, has been determined by x-ray
crystallography. An electron density map of the bovine protein was calculated at
a nominal resolution of 2.9 A by using the methods of multiple isomorphous
replacement and electron density modification refinement. The molecule is
approximately 45 X 25 X 20 A in size. Almost half of the amino acid residues
participate in two large beta structures, one of four strands and the other of
three, linked by a central disulfide bond. The molecule thus strongly resembles
Ig constant domains in polypeptide chain folding and overall tertiary structure.
Amino acid residues that are the same in the sequences of beta 2-microglobulin
and Ig constant domains are predominantly in the interior of the molecule,
whereas residues conserved among beta 2-microglobulins from different species
are both in the interior and on the molecular surface. In the crystals studied,
the molecule is clearly monomeric, consistent with the observation that beta
2-microglobulin, unlike Ig constant domains, apparently does not form dimers in
vivo but associates with the heavy chains of major histocompatibility complex
antigens. Our results demonstrate that, at the level of detailed
three-dimensional structure, the light chain of the major histocompatibility
class I antigens belongs to a superfamily of structures related to the Ig
constant domains.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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B.Pavone,
S.Bucci,
V.Sirolli,
G.Merlini,
P.Del Boccio,
M.Di Rienzo,
P.Felaco,
L.Amoroso,
P.Sacchetta,
C.Di Ilio,
G.Federici,
A.Urbani,
and
M.Bonomini
(2011).
Beta2-microglobulin causes abnormal phosphatidylserine exposure in human red blood cells.
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| |
Mol Biosyst, 7,
651-658.
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|
C.Liu,
M.R.Sawaya,
and
D.Eisenberg
(2011).
β₂-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.
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| |
Nat Struct Mol Biol, 18,
49-55.
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T.Eichner,
A.P.Kalverda,
G.S.Thompson,
S.W.Homans,
and
S.E.Radford
(2011).
Conformational conversion during amyloid formation at atomic resolution.
|
| |
Mol Cell, 41,
161-172.
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PDB codes:
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H.Mohd-Padil,
K.Tajul-Arifin,
and
A.Mohd-Adnan
(2010).
Characterization of the functional domain of β2-microglobulin from the Asian seabass, Lates calcarifer.
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| |
PLoS One, 5,
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J.P.Hodkinson,
T.R.Jahn,
S.E.Radford,
and
A.E.Ashcroft
(2009).
HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein beta(2)-microglobulin upon release from the MHC-1.
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| |
J Am Soc Mass Spectrom, 20,
278-286.
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S.Yu,
X.Chen,
and
J.Ao
(2009).
Molecular characterization and expression analysis of beta2-microglobulin in large yellow croaker Pseudosciaena crocea.
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| |
Mol Biol Rep, 36,
1715-1723.
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W.Chen,
F.Chu,
H.Peng,
J.Zhang,
J.Qi,
F.Jiang,
C.Xia,
and
F.Gao
(2008).
Expression, purification, crystallization and preliminary X-ray diffraction analysis of grass carp beta2-microglobulin.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun, 64,
200-202.
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|
S.Park,
and
J.G.Saven
(2006).
Simulation of pH-dependent edge strand rearrangement in human beta-2 microglobulin.
|
| |
Protein Sci, 15,
200-207.
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|
Y.Motomiya,
Y.Ando,
K.Haraoka,
X.Sun,
H.Morita,
I.Amano,
T.Uchimura,
and
I.Maruyama
(2005).
Studies on unfolded beta-microglobulin at C-terminal in dialysis-related amyloidosis.
|
| |
Kidney Int, 67,
314-320.
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E.S.Jordanova,
S.A.Riemersma,
K.Philippo,
E.Schuuring,
and
P.M.Kluin
(2003).
Beta2-microglobulin aberrations in diffuse large B-cell lymphoma of the testis and the central nervous system.
|
| |
Int J Cancer, 103,
393-398.
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C.H.Trinh,
D.P.Smith,
A.P.Kalverda,
S.E.Phillips,
and
S.E.Radford
(2002).
Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties.
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| |
Proc Natl Acad Sci U S A, 99,
9771-9776.
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PDB code:
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G.Verdone,
A.Corazza,
P.Viglino,
F.Pettirossi,
S.Giorgetti,
P.Mangione,
A.Andreola,
M.Stoppini,
V.Bellotti,
and
G.Esposito
(2002).
The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition.
|
| |
Protein Sci, 11,
487-499.
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PDB code:
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E.Balint
(2001).
Role of beta(2)-microglobulin in the immune response in renal osteodystrophy.
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Semin Dial, 14,
113-116.
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K.Ohashi
(2001).
Pathogenesis of beta2-microglobulin amyloidosis.
|
| |
Pathol Int, 51,
1.
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|
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Y.Hirakura,
and
B.L.Kagan
(2001).
Pore formation by beta-2-microglobulin: a mechanism for the pathogenesis of dialysis associated amyloidosis.
|
| |
Amyloid, 8,
94.
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N.A.Hoenich,
and
S.Stamp
(2000).
Clinical investigation of the role of membrane structure on blood contact and solute transport characteristics of a cellulose membrane.
|
| |
Biomaterials, 21,
317-324.
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N.Sakata,
Y.Sasatomi,
S.Ando,
J.Meng,
Y.Imanaga,
N.Uesugi,
and
S.Takebayashi
(2000).
Causal relationship between conformational change and inhibition of domain functions of glycoxidative fibronectin.
|
| |
Connect Tissue Res, 41,
117-129.
|
|
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|
|
S.M.Sprague,
and
M.M.Popovtzer
(1995).
Is beta 2-microglobulin a mediator of bone disease?
|
| |
Kidney Int, 47,
1-6.
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W.R.Clark,
W.L.Macias,
B.A.Molitoris,
and
N.H.Wang
(1995).
Plasma protein adsorption to highly permeable hemodialysis membranes.
|
| |
Kidney Int, 48,
481-488.
|
|
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|
|
|
|
B.Rubin,
J.Arnaud,
S.Caspar-Bauguil,
F.Conte,
and
A.Huchenq
(1994).
Biological function of the extracellular domain of the T-cell receptor constant region.
|
| |
Scand J Immunol, 39,
517-525.
|
|
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|
H.Ono,
F.Figueroa,
C.O'hUigin,
and
J.Klein
(1993).
Cloning of the beta 2-microglobulin gene in the zebrafish.
|
| |
Immunogenetics, 38,
1.
|
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K.C.Sato,
M.Kumakiri,
H.Koizumi,
M.Ando,
A.Ohkawara,
Y.Fujioka,
and
T.Kon
(1993).
Lichenoid skin lesions as a sign of beta 2-microglobulin-induced amyloidosis in a long-term haemodialysis patient.
|
| |
Br J Dermatol, 128,
686-689.
|
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|
D.A.Lawlor,
and
P.Parham
(1992).
Structure of CD8 alpha and beta chains of the orangutan: novel patterns of mRNA splicing encoding hingeless polypeptides.
|
| |
Immunogenetics, 36,
121-125.
|
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J.M.Campistol,
T.Shirahama,
C.R.Abraham,
O.G.Rodgers,
M.Solé,
A.S.Cohen,
and
M.Skinner
(1992).
Demonstration of plasma proteinase inhibitors in beta 2-microglobulin amyloid deposits.
|
| |
Kidney Int, 42,
915-923.
|
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J.M.Greve,
C.P.Forte,
C.W.Marlor,
A.M.Meyer,
H.Hoover-Litty,
D.Wunderlich,
and
A.McClelland
(1991).
Mechanisms of receptor-mediated rhinovirus neutralization defined by two soluble forms of ICAM-1.
|
| |
J Virol, 65,
6015-6023.
|
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|
C.P.Maury
(1990).
beta 2-Microglobulin amyloidosis. A systemic amyloid disease affecting primarily synovium and bone in long-term dialysis patients.
|
| |
Rheumatol Int, 10,
1-8.
|
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M.Barbu
(1990).
Molecular cloning of cDNAs that encode the chicken P0 protein: evidence for early expression in avians.
|
| |
J Neurosci Res, 25,
143-151.
|
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|
J.C.Gorga,
A.Dong,
M.C.Manning,
R.W.Woody,
W.S.Caughey,
and
J.L.Strominger
(1989).
Comparison of the secondary structures of human class I and class II major histocompatibility complex antigens by Fourier transform infrared and circular dichroism spectroscopy.
|
| |
Proc Natl Acad Sci U S A, 86,
2321-2325.
|
|
|
|
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|
|
J.G.Dohlman,
H.De Loof,
M.Prabhakaran,
W.J.Koopman,
and
J.P.Segrest
(1989).
Identification of peptide hormones of the amphipathic helix class using the helical hydrophobic moment algorithm.
|
| |
Proteins, 6,
61-69.
|
|
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|
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|
|
J.W.Becker,
H.P.Erickson,
S.Hoffman,
B.A.Cunningham,
and
G.M.Edelman
(1989).
Topology of cell adhesion molecules.
|
| |
Proc Natl Acad Sci U S A, 86,
1088-1092.
|
|
|
|
|
|
|
K.S.Kleinman,
and
J.W.Coburn
(1989).
Amyloid syndromes associated with hemodialysis.
|
| |
Kidney Int, 35,
567-575.
|
|
|
|
|
|
|
M.C.Nieto,
E.S.Song,
D.McKinney,
M.McMillan,
and
R.S.Goodenow
(1989).
The association of H-2Ld with human beta-2 microglobulin induces localized conformational changes in the alpha-1 and -2 superdomain.
|
| |
Immunogenetics, 30,
361-369.
|
|
|
|
|
|
|
J.Sundelin,
L.Björck,
and
L.Lögdberg
(1988).
The complete amino acid sequence of rat beta 2-microglobulin.
|
| |
Scand J Immunol, 27,
195-199.
|
|
|
|
|
|
|
G.M.Edelman
(1987).
CAMs and Igs: cell adhesion and the evolutionary origins of immunity.
|
| |
Immunol Rev, 100,
11-45.
|
|
|
|
|
|
|
L.K.Clayton,
P.H.Sayre,
J.Novotny,
and
E.L.Reinherz
(1987).
Murine and human T11 (CD2) cDNA sequences suggest a common signal transduction mechanism.
|
| |
Eur J Immunol, 17,
1367-1370.
|
|
|
|
|
|
|
M.J.Darsley,
H.Takahashi,
M.J.Macchi,
J.A.Frelinger,
K.Ozato,
and
E.Appella
(1987).
New family of exon-shuffled recombinant genes reveals extensive interdomain interactions in class I histocompatibility antigens and identifies residues involved.
|
| |
J Exp Med, 165,
211-222.
|
|
|
|
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|
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T.Matsunaga,
and
N.Mori
(1987).
The origin of the immune system. The possibility that immunoglobulin superfamily molecules and cell adhesion molecules of chicken and slime mould are all related.
|
| |
Scand J Immunol, 25,
485-495.
|
|
|
|
|
|
|
W.A.Jefferies,
and
G.G.MacPherson
(1987).
Expression of the W6/32 HLA epitope by cells of rat, mouse, human and other species: critical dependence on the interaction of specific MHC heavy chains with human or bovine beta 2-microglobulin.
|
| |
Eur J Immunol, 17,
1257-1263.
|
|
|
|
|
|
|
F.Gejyo,
S.Odani,
T.Yamada,
N.Honma,
H.Saito,
Y.Suzuki,
Y.Nakagawa,
H.Kobayashi,
Y.Maruyama,
and
Y.Hirasawa
(1986).
Beta 2-microglobulin: a new form of amyloid protein associated with chronic hemodialysis.
|
| |
Kidney Int, 30,
385-390.
|
|
|
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|
|
|
J.Novotný,
S.Tonegawa,
H.Saito,
D.M.Kranz,
and
H.N.Eisen
(1986).
Secondary, tertiary, and quaternary structure of T-cell-specific immunoglobulin-like polypeptide chains.
|
| |
Proc Natl Acad Sci U S A, 83,
742-746.
|
|
|
|
|
|
|
P.D.Gorevic,
P.C.Munoz,
T.T.Casey,
C.R.DiRaimondo,
W.J.Stone,
F.C.Prelli,
M.M.Rodrigues,
M.D.Poulik,
and
B.Frangione
(1986).
Polymerization of intact beta 2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis.
|
| |
Proc Natl Acad Sci U S A, 83,
7908-7912.
|
|
|
|
|
|
|
P.D.Gorevic,
T.T.Casey,
W.J.Stone,
C.R.DiRaimondo,
F.C.Prelli,
and
B.Frangione
(1985).
Beta-2 microglobulin is an amyloidogenic protein in man.
|
| |
J Clin Invest, 76,
2425-2429.
|
|
|
|
|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
