1a7b: Difference between revisions

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[[Image:1a7b.gif|left|200px]]
{{Seed}}
[[Image:1a7b.png|left|200px]]


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{{STRUCTURE_1a7b|  PDB=1a7b  |  SCENE=  }}  
{{STRUCTURE_1a7b|  PDB=1a7b  |  SCENE=  }}  


'''ENGINEERING A MISFOLDED FORM OF CD2'''
===ENGINEERING A MISFOLDED FORM OF CD2===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_9731771}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9731771 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9731771}}


==About this Structure==
==About this Structure==
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[[Category: Protein evolution]]
[[Category: Protein evolution]]
[[Category: Protein folding]]
[[Category: Protein folding]]
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