1a4j: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
caption="1a4j, resolution 2.1&Aring;" />
caption="1a4j, resolution 2.1&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A4J OCA].  
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.E.]]
[[Category: Romesburg, F E.]]
[[Category: Schultz, P.G.]]
[[Category: Schultz, P G.]]
[[Category: Spiller, B.W.]]
[[Category: Spiller, B W.]]
[[Category: Stevens, R.C.]]
[[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://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:47 2008''