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Three-dimensional Solution Structure Of The B Domain Of Staphylococcal Protein A: Comparisons Of The Solution And Crystal Structures.
H. Gouda, H. Torigoe, A. Saito, M. Sato, Y. Arata, I. Shimada
Published 1992 · Chemistry, Medicine
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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)
This paper references
Solution conformations of human growth hormone releasing factor: comparison of the restrained molecular dynamics and distance geometry methods for a system without long-range distance data.
A. Brünger (1987)
New methods for the measurement of NHCαH coupling constants in 15N-labeled proteins
L. Kay (1990)
Protein A of Staphylococcus aureus and related immunoglobulin receptors produced by streptococci and pneumonococci.
Langone Jj (1982)
P.E.COSY, a simple alternative to E.COSY
L. Mueller (1987)
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.
H. Torigoe (1990)
Heteronuclear nuclear magnetic resonance experiments for studies of protein conformation.
G. Wagner (1989)
A two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants☆
D. J. States (1982)
Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints.
G. Montelione (1992)
Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin c.
S. Hyberts (1987)
Low resolution structure of interleukin-1 beta in solution derived from 1H-15N heteronuclear three-dimensional nuclear magnetic resonance spectroscopy.
G. Clore (1990)
Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance.
K. Wüthrich (1983)
Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins.
D. Marion (1983)
Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution.
J. Deisenhofer (1981)
Three-dimensional structure of interleukin 8 in solution.
G. Clore (1990)
Spatially constrained minimization of macromolecules
Robert E. Bruccoleri (1986)
A powerful method of sequential proton resonance assignment in proteins using relayed 15N‐1H multiple quantum coherence spectroscopy
A. Gronenborn (1989)
Repetitive Sequences in Protein A from Staphylococcus aureus
J. Sjödahl (1977)
Determination of three‐dimensional structures of proteins from interproton distance data by hybrid distance geometry‐dynamical simulated annealing calculations
M. Nilges (1988)
Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-sepharose.
P. Ey (1978)
Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN.
G. Wagner (1987)
Tropomyosin coiled-coil interactions: evidence for an unstaggered structure.
A. McLachlan (1975)
Staphylococcal protein A consists of five IgG-binding domains.
T. Moks (1986)
High level expression of a synthetic gene coding for IgG-binding domain B of Staphylococcal protein A.
A. Saito (1989)
Investigation of exchange processes by two‐dimensional NMR spectroscopy
J. Jeener (1979)
Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
G. Bodenhausen (1980)
Viewing the energy optimization of chemical models with computer animation
J. T. Egan (1983)
Structural studies on the four repetitive Fc-binding regions in protein A from Staphylococcus aureus.
J. Sjödahl (1977)
The theory and practice of distance geometry
T. Havel (1983)
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W. Delano (2000)
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Thomas A. Knotts (2008)
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First-principles calculation of the folding free energy of a three-helix bundle protein.
E. M. Boczko (1995)
Structures of bacterial immunoglobulin-binding domains and their complexes with immunoglobulins.
M. Tashiro (1995)
Crucial importance of the water-entropy effect in predicting hot spots in protein-protein complexes.
Hiraku Oshima (2011)
Identification of peptides that bind to the constant region of a humanized IgG1 monoclonal antibody using phage display
G. Ehrlich (1998)
A new method for the preparation of unprotected peptides on biocompatible resins with application in combinatorial chemistry.
J. J. Pastor (2002)
Local structure formation in simulations of two small proteins.
G. Jayachandran (2007)
All-atom simulations of protein folding and unfolding.
R. Day (2003)
Protein H — a surface protein of Streptococcus pyogenes with separate binding sites for lgG and albumin
I. M. Frick (1994)
Structural Stability of the Coiled-Coil Domain of Tumor Susceptibility Gene (TSG)-101
Jordan T White (2017)
One-dimensional potential barrier model of protein folding with intermediates
B. Jun (2002)
Structure and stability of a model three‐helix‐bundle protein on tailored surfaces
T. A. Knotts (2005)
5 Purification Systems Based on Bacterial Surface Proteins
T. Boström (2012)
Exploring host-pathogen interactions through protein microarray. Large-scale protein microarray analysis revealed novel human receptors for the staphylococcal immune evasion protein FLIPr and for the neisserial adhesin NadA
Luigi Scietti (2015)
Multiscale conformational heterogeneity in staphylococcal protein a: possible determinant of functional plasticity.
L. Deis (2014)
Antibody variable region binding by Staphylococcal protein A: Thermodynamic analysis and location of the Fv binding site on E‐domain
M. Starovasnik (1999)
Development of a covalent site-specific antibody labeling strategy by the use of photoactivable Z domains
Anna Konrad (2012)
Quantifying hub-like behavior in protein folding networks.
A. Dickson (2012)
Analysis and design of three-stranded coiled coils and three-helix bundles.
J. Schneider (1998)
Solution structure of the albumin-binding GA module: a versatile bacterial protein domain.
M. Johansson (1997)
Plasma Half-life Extension of Small Recombinant Antibodies by Fusion to Immunoglobulin-binding Domains*
M. Hutt (2011)
13C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G
K. Kato (1993)
A kinetic mechanism for in vivo protein folding
L. Cruzeiro (2014)
Outline of an experimental design aimed to detect protein A mirror image in solution
O. A. Martin (2019)
Identification of model peptides as affinity ligands for the purification of humanized monoclonal antibodies by means of phage display.
G. Ehrlich (2001)
A method for optimizing potential-energy functions by a hierarchical design of the potential-energy landscape: Application to the UNRES force field
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