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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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'''DIELS ALDER CATALYTIC ANTIBODY GERMLINE PRECURSOR'''<br />
'''DIELS ALDER CATALYTIC ANTIBODY GERMLINE PRECURSOR'''<br />
==Overview==
==Overview==
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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.
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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==
==Disease==
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==About this Structure==
==About this Structure==
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1A4J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A4J OCA].
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1A4J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4J OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Romesburg, F.E.]]
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[[Category: Romesburg, F E.]]
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[[Category: Schultz, P.G.]]
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[[Category: Schultz, P G.]]
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[[Category: Spiller, B.W.]]
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[[Category: Spiller, B W.]]
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[[Category: Stevens, R.C.]]
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[[Category: Stevens, R C.]]
[[Category: antibody]]
[[Category: antibody]]
[[Category: catalytic antibody]]
[[Category: catalytic antibody]]
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[[Category: immunoglobulin]]
[[Category: immunoglobulin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 15:55:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:47 2008''

Revision as of 09:40, 21 February 2008


1a4j, resolution 2.1Å

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 11:40:47 2008

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