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PDBsum entry 4bjl
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Immunoglobulin
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PDB id
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4bjl
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Three quaternary structures for a single protein.
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Authors
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D.B.Huang,
C.F.Ainsworth,
F.J.Stevens,
M.Schiffer.
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Ref.
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Proc Natl Acad Sci U S A, 1996,
93,
7017-7021.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
92%.
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Abstract
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The structure of a multisubunit protein (immunoglobulin light chain) was solved
in three crystal forms, differing only in the solvent of crystallization. The
three structures were obtained at high ionic strength and low pH, high ionic
strength and high pH, and low ionic strength and neutral pH. The three resulting
"snapshots" of possible structures show that their variable-domain interactions
differ, reflecting their stabilities under specific solvent conditions. In the
three crystal forms, the variable domains had different rotational and
translational relationships, whereas no alteration of the constant domains was
found. The critical residues involved in the observed effect of the solvent are
tryptophans and histidines located between the two variable domains in the
dimeric structure. Tryptophan residues are commonly found in interfaces between
proteins and their subunits, and histidines have been implicated in pH-dependent
conformation changes. The quaternary structure observed for a multisubunit
protein or protein complex in a crystal may be influenced by the interactions of
the constituents within the molecule or complex and/or by crystal packing
interactions. The comparison of buried surface areas and hydrogen bonds between
the domains forming the molecule and between the molecules forming the crystals
suggest that, for this system, the interactions within the molecule are most
likely the determining factors.
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Secondary reference #1
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Title
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Structure of a second crystal form of bence-Jones protein loc: strikingly different domain associations in two crystal forms of a single protein.
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Authors
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M.Schiffer,
C.Ainsworth,
Z.B.Xu,
W.Carperos,
K.Olsen,
A.Solomon,
F.J.Stevens,
C.H.Chang.
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Ref.
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Biochemistry, 1989,
28,
4066-4072.
[DOI no: ]
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PubMed id
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