Difference between revisions of "Part:BBa K1497024"
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       <p class="MsoCaption" align="text-align:justify"><span lang="EN-US"><b>Figure 1</b></span></a><span lang="EN-US">
 
       <p class="MsoCaption" align="text-align:justify"><span lang="EN-US"><b>Figure 1</b></span></a><span lang="EN-US">
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Crystal structure of the GBD domain from the N-WASP protein (red) of Rattus rattus binding the small molecule Wiskostatin (1-(3,6-Dibromo-carbazol-9-yl)-3-dimethylamino-propan-2-ol).  The GBD domain is locked by Wiskostatin in its autoinhibited binding conformation (Peterson et al. 2004). PDB entry 1T84.</span></p>
 
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====References====
 
====References====
 
Dueber, John E.; Wu, Gabriel C.; Malmirchegini, G. Reza; Moon, Tae Seok; Petzold, Christopher J.; Ullal, Adeeti V. et al. (2009): Synthetic protein scaffolds provide modular control over metabolic flux. In Nat. Biotechnol. 27 (8), pp. 753–759. DOI: 10.1038/nbt.1557.
 
Dueber, John E.; Wu, Gabriel C.; Malmirchegini, G. Reza; Moon, Tae Seok; Petzold, Christopher J.; Ullal, Adeeti V. et al. (2009): Synthetic protein scaffolds provide modular control over metabolic flux. In Nat. Biotechnol. 27 (8), pp. 753–759. DOI: 10.1038/nbt.1557.
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<br>
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<br><br>
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Kim, A. S.; Kakalis, L. T.; Abdul-Manan, N.; Liu, G. A.; Rosen, M. K. (2000): Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. In Nature 404 (6774), pp. 151–158. DOI: 10.1038/35004513.
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Kim, A. S.; Kakalis, L. T.; Abdul-Manan, N.; Liu, G. A.; Rosen, M. K. (2000): Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. In Nature 404 (6774), pp. 151–158. DOI: 10.1038/35004513. <br><br>
 +
Peterson, Jeffrey R.; Bickford, Lincoln C.; Morgan, David; Kim, Annette S.; Ouerfelli, Ouathek; Kirschner, Marc W.; Rosen, Michael K. (2004): Chemical inhibition of N-WASP by stabilization of a native autoinhibited conformation. In Nat. Struct. Mol. Biol. 11 (8), pp. 747–755. DOI: 10.1038/nsmb796.

Revision as of 19:13, 11 October 2014

GBD-Domain

The GBD domain and its ligand (BBa_K771106) are suitable tools for protein colocalizaion. Initially, the domain was a part of the N-WASP protein (GTPase binding domain) in Rattus rattus. The GBD domain is used as a binding unit of the so-called protein scaffold published by Dueber et al. in 2012. The scaffold (BBa_K1497033) is composed of different binding units, which enable the assembly of multiple target proteins. This BioBrick adds a BglII and BamHI restriction site in front of and behind the previously constructed domain sequence (BBa_K771105). Now, different binding units of the scaffold protein can be fused together without the introduction of restriction sites. This allows the easy construction of BioBricks of different permutations of the scaffold protein domains.

Figure 1 Crystal structure of the GBD domain from the N-WASP protein (red) of Rattus rattus binding the small molecule Wiskostatin (1-(3,6-Dibromo-carbazol-9-yl)-3-dimethylamino-propan-2-ol). The GBD domain is locked by Wiskostatin in its autoinhibited binding conformation (Peterson et al. 2004). PDB entry 1T84.
Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


References

Dueber, John E.; Wu, Gabriel C.; Malmirchegini, G. Reza; Moon, Tae Seok; Petzold, Christopher J.; Ullal, Adeeti V. et al. (2009): Synthetic protein scaffolds provide modular control over metabolic flux. In Nat. Biotechnol. 27 (8), pp. 753–759. DOI: 10.1038/nbt.1557.

Kim, A. S.; Kakalis, L. T.; Abdul-Manan, N.; Liu, G. A.; Rosen, M. K. (2000): Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. In Nature 404 (6774), pp. 151–158. DOI: 10.1038/35004513.

Peterson, Jeffrey R.; Bickford, Lincoln C.; Morgan, David; Kim, Annette S.; Ouerfelli, Ouathek; Kirschner, Marc W.; Rosen, Michael K. (2004): Chemical inhibition of N-WASP by stabilization of a native autoinhibited conformation. In Nat. Struct. Mol. Biol. 11 (8), pp. 747–755. DOI: 10.1038/nsmb796.