1a4j

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(New page: 200px<br /> <applet load="1a4j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a4j, resolution 2.1&Aring;" /> '''DIELS ALDER CATALYTI...)
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Revision as of 13:49, 12 November 2007


1a4j, resolution 2.1Å

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DIELS ALDER CATALYTIC ANTIBODY GERMLINE PRECURSOR

Contents

Overview

The three-dimensional structure of an antibody (39-A11) that catalyzes a, Diels-Alder reaction has been determined. The structure suggests that the, antibody catalyzes this pericyclic reaction through a combination of, packing and hydrogen-bonding interactions that control the relative, geometries of the bound substrates and electronic distribution in the, dienophile. A single somatic mutation, serine-91 of the light chain to, valine, is largely responsible for the increase in affinity and catalytic, activity of the affinity-matured antibody. Structural and functional, studies of the germ-line precursor suggest that 39-A11 and related, antibodies derive from a family of germ-line genes that have been selected, throughout evolution for the ability of the encoded proteins to form a, polyspecific combining site. Germ line-encoded antibodies of this type, which can rapidly evolve into high-affinity receptors for a broad range of, structures, may help to expand the binding potential associated with the, structural diversity of the primary antibody repertoire.

Disease

Known disease associated with this structure: Kappa light chain deficiency OMIM:[147200]

About this Structure

1A4J is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Immunological origins of binding and catalysis in a Diels-Alderase antibody., Romesberg FE, Spiller B, Schultz PG, Stevens RC, Science. 1998 Mar 20;279(5358):1929-33. PMID:9506942

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