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PDBsum entry 1bdd
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Immunoglobulin-binding protein
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PDB id
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1bdd
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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-Dimensional solution structure of the b domain of staphylococcal protein a: comparisons of the solution and crystal structures.
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Authors
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H.Gouda,
H.Torigoe,
A.Saito,
M.Sato,
Y.Arata,
I.Shimada.
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Ref.
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Biochemistry, 1992,
31,
9665-9672.
[DOI no: ]
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PubMed id
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Abstract
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The three-dimensional solution structure of the recombinant B domain (FB) of
staphylococcal protein A, which specifically binds to the Fc portion of
immunoglobulin G, was determined by NMR spectroscopy and hybrid distance
geometry-dynamical simulated annealing calculations. On the basis of 692
experimental constraints including 587 distance constraints obtained from the
nuclear Overhauser effect (NOE), 57 torsion angle (phi, chi 1) constraints, and
48 constraints associated with 24 hydrogen bonds, a total of 10 converged
structures of FB were obtained. The atomic root mean square difference among the
10 converged structures is 0.52 +/- 0.10 A for the backbone atoms and 0.98 +/-
0.08 A for all heavy atoms (excluding the N-terminal segment from Thr1 to Glu9
and the C-terminal segment from Gln56 to Ala60, which are partially disordered).
FB is composed of a bundle of three alpha-helices, i.e., helix I (Gln10-His19),
helix II (Glu25-Asp37), and helix III (Ser42-Ala55). Helix II and helix III are
antiparallel to each other, whereas the long axis of helix I is tilted at an
angle of about 30 degrees with respect to those of helix II and helix III. Most
of the hydrophobic residues of FB are buried in the interior of the bundle of
the three helices. It is suggested that the buried hydrophobic residues form a
hydrophobic core, contributing to the stability of FB.(ABSTRACT TRUNCATED AT 250
WORDS)
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Secondary reference #1
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Title
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15n nuclear magnetic resonance studies of the b domain of staphylococcal protein a: sequence specific assignments of the imide 15n resonances of the proline residues and the interaction with human immunoglobulin g.
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Authors
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H.Torigoe,
I.Shimada,
M.Waelchli,
A.Saito,
M.Sato,
Y.Arata.
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Ref.
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FEBS Lett, 1990,
269,
174-176.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Sequential 1h nmr assignments and secondary structure of the b domain of staphylococcal protein a: structural changes between the free b domain in solution and the fc-Bound b domain in crystal.
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Authors
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H.Torigoe,
I.Shimada,
A.Saito,
M.Sato,
Y.Arata.
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Ref.
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Biochemistry, 1990,
29,
8787-8793.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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High level expression of a synthetic gene coding for igg-Binding domain b of staphylococcal protein a.
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Authors
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A.Saito,
S.Honda,
T.Nishi,
M.Koike,
K.Okazaki,
S.Itoh,
M.Sato.
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Ref.
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Protein Eng, 1989,
2,
481-487.
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PubMed id
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