1emt: Difference between revisions
New page: left|200px<br /> <applet load="1emt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1emt, resolution 2.25Å" /> '''FAB ANTIBODY FRAGME... |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1emt.gif|left|200px]]<br /> | [[Image:1emt.gif|left|200px]]<br /><applet load="1emt" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1emt" size=" | |||
caption="1emt, resolution 2.25Å" /> | caption="1emt, resolution 2.25Å" /> | ||
'''FAB ANTIBODY FRAGMENT OF AN C60 ANTIFULLERENE ANTIBODY'''<br /> | '''FAB ANTIBODY FRAGMENT OF AN C60 ANTIFULLERENE ANTIBODY'''<br /> | ||
==Overview== | ==Overview== | ||
We have prepared a monoclonal Buckminsterfullerene specific antibody and | We have prepared a monoclonal Buckminsterfullerene specific antibody and report the sequences of its light and heavy chains. We also show, by x-ray crystallographic analysis of the Fab fragment and by model building, that the fullerene binding site is formed by the interface of the antibody light and heavy chains. Shape-complementary clustering of hydrophobic amino acids, several of which participate in putative stacking interactions with fullerene, form the binding site. Moreover, an induced fit mechanism appears to participate in the fullerene binding process. Affinity of the antibody-fullerene complex is 22 nM as measured by competitive binding. These findings should be applicable not only to the use of antibodies to assay and direct potential fullerene-based drug design but could also lead to new methodologies for the production of fullerene derivatives and nanotubes as well. | ||
==About this Structure== | ==About this Structure== | ||
1EMT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | 1EMT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1EMT OCA]. | ||
==Reference== | ==Reference== | ||
Line 14: | Line 13: | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Braden, B | [[Category: Braden, B C.]] | ||
[[Category: Chen, B | [[Category: Chen, B X.]] | ||
[[Category: Erlanger, B | [[Category: Erlanger, B F.]] | ||
[[Category: Goldbaum, F | [[Category: Goldbaum, F A.]] | ||
[[Category: Kirschner, A | [[Category: Kirschner, A N.]] | ||
[[Category: Wilson, S | [[Category: Wilson, S R.]] | ||
[[Category: anti-fullerene antibody]] | [[Category: anti-fullerene antibody]] | ||
[[Category: nanotubes]] | [[Category: nanotubes]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:29:23 2008'' |
Revision as of 13:29, 21 February 2008
|
FAB ANTIBODY FRAGMENT OF AN C60 ANTIFULLERENE ANTIBODY
OverviewOverview
We have prepared a monoclonal Buckminsterfullerene specific antibody and report the sequences of its light and heavy chains. We also show, by x-ray crystallographic analysis of the Fab fragment and by model building, that the fullerene binding site is formed by the interface of the antibody light and heavy chains. Shape-complementary clustering of hydrophobic amino acids, several of which participate in putative stacking interactions with fullerene, form the binding site. Moreover, an induced fit mechanism appears to participate in the fullerene binding process. Affinity of the antibody-fullerene complex is 22 nM as measured by competitive binding. These findings should be applicable not only to the use of antibodies to assay and direct potential fullerene-based drug design but could also lead to new methodologies for the production of fullerene derivatives and nanotubes as well.
About this StructureAbout this Structure
1EMT is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
X-ray crystal structure of an anti-Buckminsterfullerene antibody fab fragment: biomolecular recognition of C(60)., Braden BC, Goldbaum FA, Chen BX, Kirschner AN, Wilson SR, Erlanger BF, Proc Natl Acad Sci U S A. 2000 Oct 24;97(22):12193-7. PMID:11035793
Page seeded by OCA on Thu Feb 21 12:29:23 2008