1a64
From Proteopedia
(New page: 200px<br /><applet load="1a64" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a64, resolution 2.0Å" /> '''ENGINEERING A MISFOLD...) |
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| - | [[Image:1a64.gif|left|200px]]<br /><applet load="1a64" size=" | + | [[Image:1a64.gif|left|200px]]<br /><applet load="1a64" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1a64, resolution 2.0Å" /> | caption="1a64, resolution 2.0Å" /> | ||
'''ENGINEERING A MISFOLDED FORM OF RAT CD2'''<br /> | '''ENGINEERING A MISFOLDED FORM OF RAT CD2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The amino-terminal domain of CD2 has the remarkable ability to fold in two | + | The amino-terminal domain of CD2 has the remarkable ability to fold in two ways: either as a monomer or as an intertwined, metastable dimer. Here we show that it is possible to differentially stabilize either fold by engineering the CD2 sequence, mimicking random mutagenesis events that could occur during molecular evolution. Crystal structures of a hinge-deletion mutant, which is stable as an intertwined dimer, reveal domain rotations that enable the protein to further assemble to a tetramer. These results demonstrate that a variety of folds can be adopted by a single polypeptide sequence, and provide guidance for the design of proteins capable of further assembly. |
==About this Structure== | ==About this Structure== | ||
| - | 1A64 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1A64 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A64 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Barker, J | + | [[Category: Barker, J J.]] |
| - | [[Category: Brady, R | + | [[Category: Brady, R L.]] |
| - | [[Category: Head, J | + | [[Category: Head, J G.]] |
| - | [[Category: Murray, A | + | [[Category: Murray, A J.]] |
[[Category: domain swapping]] | [[Category: domain swapping]] | ||
[[Category: hinge loop]] | [[Category: hinge loop]] | ||
[[Category: oligomer evolution]] | [[Category: oligomer evolution]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:17 2008'' |
Revision as of 09:41, 21 February 2008
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ENGINEERING A MISFOLDED FORM OF RAT CD2
Overview
The amino-terminal domain of CD2 has the remarkable ability to fold in two ways: either as a monomer or as an intertwined, metastable dimer. Here we show that it is possible to differentially stabilize either fold by engineering the CD2 sequence, mimicking random mutagenesis events that could occur during molecular evolution. Crystal structures of a hinge-deletion mutant, which is stable as an intertwined dimer, reveal domain rotations that enable the protein to further assemble to a tetramer. These results demonstrate that a variety of folds can be adopted by a single polypeptide sequence, and provide guidance for the design of proteins capable of further assembly.
About this Structure
1A64 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Engineering an intertwined form of CD2 for stability and assembly., Murray AJ, Head JG, Barker JJ, Brady RL, Nat Struct Biol. 1998 Sep;5(9):778-82. PMID:9731771
Page seeded by OCA on Thu Feb 21 11:41:17 2008
