1a4j
From Proteopedia
(New page: 200px<br /> <applet load="1a4j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a4j, resolution 2.1Å" /> '''DIELS ALDER CATALYTI...) |
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- | [[Image:1a4j.gif|left|200px]]<br /> | + | [[Image:1a4j.gif|left|200px]]<br /><applet load="1a4j" size="350" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="1a4j" size=" | + | |
caption="1a4j, resolution 2.1Å" /> | caption="1a4j, resolution 2.1Å" /> | ||
'''DIELS ALDER CATALYTIC ANTIBODY GERMLINE PRECURSOR'''<br /> | '''DIELS ALDER CATALYTIC ANTIBODY GERMLINE PRECURSOR'''<br /> | ||
==Overview== | ==Overview== | ||
- | The three-dimensional structure of an antibody (39-A11) that catalyzes a | + | 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== | ||
- | 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:// | + | 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]] | ||
- | [[Category: Romesburg, F | + | [[Category: Romesburg, F E.]] |
- | [[Category: Schultz, P | + | [[Category: Schultz, P G.]] |
- | [[Category: Spiller, B | + | [[Category: Spiller, B W.]] |
- | [[Category: Stevens, R | + | [[Category: Stevens, R C.]] |
[[Category: antibody]] | [[Category: antibody]] | ||
[[Category: catalytic antibody]] | [[Category: catalytic antibody]] | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
- | ''Page seeded by [http:// | + | ''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
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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
Page seeded by OCA on Thu Feb 21 11:40:47 2008