1a64: Difference between revisions

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[[Image:1a64.gif|left|200px]]<br /><applet load="1a64" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1a64.gif|left|200px]]
caption="1a64, resolution 2.0&Aring;" />
 
'''ENGINEERING A MISFOLDED FORM OF RAT CD2'''<br />
{{Structure
|PDB= 1a64 |SIZE=350|CAPTION= <scene name='initialview01'>1a64</scene>, resolution 2.0&Aring;
|SITE=
|LIGAND=
|ACTIVITY=
|GENE=
}}
 
'''ENGINEERING A MISFOLDED FORM OF RAT CD2'''
 


==Overview==
==Overview==
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==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://oca.weizmann.ac.il/oca-bin/ocashort?id=1A64 OCA].  
1A64 is a [[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==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9731771 9731771]
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:[http://www.ncbi.nlm.nih.gov/pubmed/9731771 9731771]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: oligomer evolution]]
[[Category: oligomer evolution]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:17 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:53:29 2008''

Revision as of 10:53, 20 March 2008

File:1a64.gif


PDB ID 1a64

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, resolution 2.0Å
Coordinates: save as pdb, mmCIF, xml



ENGINEERING A MISFOLDED FORM OF RAT CD2


OverviewOverview

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 StructureAbout this Structure

1A64 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

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 Mar 20 09:53:29 2008

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