Biological Unit: Difference between revisions
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4 | 4 | ||
</center></td><td><center> | </center></td><td><center> | ||
4, 4, 2, 2 | 4**, 4*, 2, 2 | ||
</center></td></tr><tr><td><center> | </center></td></tr><tr><td><center> | ||
[[3dxp]]<br>[[1hho]]<br>[[3dxr]] | [[3dxp]]<br>[[1hho]]<br>[[3dxr]] | ||
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</center></td></tr> | </center></td></tr> | ||
</table> | </table> | ||
* The contacts in | * The contacts in this biological unit differ from those in the asymmetric unit. | ||
<br>**The "author specified" | <br>**The "author specified" assembly (in this case the same as the [[asymmetric unit]]) appears unlikely in view of the assembly predicted by [[#Protein Interfaces, Surfaces and Assemblies Server (PISA)|PISA]], which has a much larger buried surface area. | ||
</center> | </center> | ||
Truncated proteins may form oligomers that are impossible in the native protein. For example, [[1bk5]] (karyopherin alpha) is a truncated part of the natural chain, and forms a dimer that would be prevented by the full-length chain. Dimerization is dependent upon Y397. Mutation Y397D prevents this artifactual dimerization, leading to the monomer [[1ee5]]. | Truncated proteins may form oligomers that are impossible in the native protein. For example, [[1bk5]] (karyopherin alpha) is a truncated part of the natural chain, and forms a dimer that would be prevented by the full-length chain. Dimerization is dependent upon Y397. Mutation Y397D prevents this artifactual dimerization, leading to the monomer [[1ee5]]. | ||
