Sequential sup 1 H NMR assignments and secondary structure of an IgG-binding domain from protein G

Protein G is a member of a class of cell surface bacterial proteins from Streptococcus that bind IgG with high affinity. A fragment of molecular mass 6,988, which retains IgG-binding activity, has been generated by proteolytic digestion and analyzed by {sup 1}H NMR. Two-dimenstional DQF-COSY, TOCSY,...

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Bibliographic Details
Published in:Biochemistry (Easton) 1991-06, Vol.30:22
Main Authors: Lian, L.Y., Yang, J.C., Derrick, J.P., Sutcliffe, M.J., Roberts, G.C.K., Murphy, J.P., Goward, C.R., Atkinson, T.
Format: Article
Language:English
Subjects:
550601 - Medicine- Unsealed Radionuclides in Diagnostics
ALANINES
AMINO ACIDS
ASPARTIC ACID
BACTERIA
BARYONS
CARBOXYLIC ACIDS
CHEMICAL SHIFT
ELEMENTARY PARTICLES
FERMIONS
GLOBULINS
HADRONS
IMMUNOGLOBULINS
MAGNETIC RESONANCE
MEMBRANE PROTEINS
MICROORGANISMS
NUCLEAR MAGNETIC RESONANCE
NUCLEONS
ORGANIC ACIDS
ORGANIC COMPOUNDS
OVERHAUSER EFFECT
PROTEINS
PROTONS
RADIOLOGY AND NUCLEAR MEDICINE
RESONANCE
STREPTOCOCCUS
VALINE
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Summary:Protein G is a member of a class of cell surface bacterial proteins from Streptococcus that bind IgG with high affinity. A fragment of molecular mass 6,988, which retains IgG-binding activity, has been generated by proteolytic digestion and analyzed by {sup 1}H NMR. Two-dimenstional DQF-COSY, TOCSY, and NOESY spectra have been employed to assign the {sup 1}H NMR spectrum of the peptide. Elements of regular secondary structure have been identified by using nuclear Overhauser enhancement, coupling constant, and amide proton exchange data. The secondary structure consists of a central {alpha}-helix (Ala28-Val44), flanked by two portions of {beta}-sheet (Val5-Val26 and Asp45-Lys62). This is a fundamentally different arrangement of secondary structure from that of protein A, which is made up of three consecutive {alpha}-helics in free solution. The authors conclude that the molecular mechanisms underlying the association of protein A and protein G with IgG are different.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00236a002