Proton nuclear magnetic resonance sequential assignments and secondary structure of an immunoglobulin light chain-binding domain of protein L

M. Wikström, U. Sjöbring, W. Kastern, Lars Björk, Torbjörn Drakenberg, Sture Forsen

Research output: Contribution to journalArticleScientificpeer-review

45 Citations (Scopus)

Abstract

The 1H NMR assignments have been made for the immunoglobulin (Ig) light chain-binding B1 domain of protein L from Peptostreptococcus magnus. The secondary structure elements and the global folding pattern were determined from nuclear Overhauser effects, backbone coupling constants, and slowly exchanging amide protons. The B1 domain was found to be folded into a globular unit of 61 amino acid residues, preceded by a 15 amino acid long disordered N-terminus. The folded portion of the molecule contains a four-stranded beta-sheet spanned by a central alpha-helix. The fold is similar to the IgG-binding domains of streptococcal protein G, despite the fact that the binding sites on immunoglobulins for the two proteins are different; protein G binds IgG through the constant (Fc) part of the heavy chain, whereas protein L has affinity for the variable domain of Ig light chains.
Original languageEnglish
Pages (from-to)3381 - 3386
Number of pages6
JournalBiochemistry
Volume32
DOIs
Publication statusPublished - 1993
MoE publication typeA1 Journal article-refereed

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Immunoglobulin Light Chains
Protons
Carrier Proteins
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Immunoglobulin G
Amino Acids
Proteins
Amides
Immunoglobulins
Binding Sites
Molecules

Cite this

Wikström, M. ; Sjöbring, U. ; Kastern, W. ; Björk, Lars ; Drakenberg, Torbjörn ; Forsen, Sture. / Proton nuclear magnetic resonance sequential assignments and secondary structure of an immunoglobulin light chain-binding domain of protein L. In: Biochemistry. 1993 ; Vol. 32. pp. 3381 - 3386.
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Proton nuclear magnetic resonance sequential assignments and secondary structure of an immunoglobulin light chain-binding domain of protein L. / Wikström, M.; Sjöbring, U.; Kastern, W.; Björk, Lars; Drakenberg, Torbjörn; Forsen, Sture.

In: Biochemistry, Vol. 32, 1993, p. 3381 - 3386.

Research output: Contribution to journalArticleScientificpeer-review

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AU - Wikström, M.

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AU - Forsen, Sture

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AB - The 1H NMR assignments have been made for the immunoglobulin (Ig) light chain-binding B1 domain of protein L from Peptostreptococcus magnus. The secondary structure elements and the global folding pattern were determined from nuclear Overhauser effects, backbone coupling constants, and slowly exchanging amide protons. The B1 domain was found to be folded into a globular unit of 61 amino acid residues, preceded by a 15 amino acid long disordered N-terminus. The folded portion of the molecule contains a four-stranded beta-sheet spanned by a central alpha-helix. The fold is similar to the IgG-binding domains of streptococcal protein G, despite the fact that the binding sites on immunoglobulins for the two proteins are different; protein G binds IgG through the constant (Fc) part of the heavy chain, whereas protein L has affinity for the variable domain of Ig light chains.

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