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Structure-function relations in phosphorylcholine-binding mouse myeloma proteins

Goetze, Andrew M. and Richards, John H. (1977) Structure-function relations in phosphorylcholine-binding mouse myeloma proteins. Proceedings of the National Academy of Sciences of the United States of America, 74 (5). pp. 2109-2112. ISSN 0027-8424.

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The binding site interactions between the phosphorylcholine (phosphocholine)-binding mouse myeloma proteins TEPC 15, W3207, McPC 603, MOPC 167, and MOPC 511 and the isotopically substituted hapten phosphoryl-[methyl-13C]choline have been investigated using 13C and 31P nuclear magnetic resonance (NMR) spectroscopy. Each protein exhibits a unique NMR pattern, but extensive similarities in chemical shift parameters upon binding of hapten to immunoglobulin suggest a significant degree of conservation of important hapten-binding site interactions. Moreover, independent binding studies, in conjunction with the NMR data, allow construction of a simple model of the binding sites of these antibodies, analyzed in terms of the relative strength of interaction between hapten and two main subsites. The NMR evidence supports the view that the heavy chains of these proteins dominate in interacting with bound phosphorylcholine; the various subspecificities of these proteins for phosphorylcholine analogues can be accounted for by amino acid changes in the hypervariable regions of the heavy chains.

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Additional Information:© 1977 by the National Academy of Sciences. Communicated by Ray D. Owen, March 7, 1977. This is Contribution 5452 from the Division of Chemistry and Chemical Engineering, California Institute of Technology. The costs of publication of this article were defrayed in part by the payment of page charges from funds made available to support the research which is the subject of the article. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Subject Keywords:nuclear magnetic resonance; binding subsites; hapten environment
Issue or Number:5
Record Number:CaltechAUTHORS:GOEpnas77
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:8089
Deposited By: Tony Diaz
Deposited On:01 Aug 2007
Last Modified:02 Oct 2019 23:48

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