2v7g: Difference between revisions

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[[Image:2v7g.~~jpg~~|left|200px]]

[[Image:2v7g.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF AN ENGINEERED UROCANASE TETRAMER~~'''~~

===CRYSTAL STRUCTURE OF AN ENGINEERED UROCANASE TETRAMER===

~~==Overview==~~

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The analysis of natural contact interfaces between protein subunits and between proteins has disclosed some general rules governing their association. We have applied these rules to produce a number of novel assemblies, ~~demonstrating that a given protein can be engineered~~ to ~~form contacts~~ at ~~various points of its surface~~. ~~Symmetry plays an important role because it defines the multiplicity of a designed contact and therefore~~ the number ~~of required mutations~~. ~~Some of the proteins needed only a single side~~-~~chain alteration in order to associate to a higher~~-order complex. The mobility of the buried side chains has to be taken into account. Four assemblies have been structurally elucidated. Comparisons between the designed contacts and the results will provide useful guidelines for the development of future architectures.

The line below this paragraph, {{ABSTRACT_PUBMED_18187656}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18187656 is the PubMed ID number.

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==About this Structure==

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[[Category: Protein engineering]]

[[Category: Urocanate hydratase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 18~~:19:28 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:17:46 2008''

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-[[Image:2v7g.jpg|left|200px]]
+{{Seed}}
+[[Image:2v7g.png|left|200px]]
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 {{STRUCTURE_2v7g|  PDB=2v7g  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF AN ENGINEERED UROCANASE TETRAMER'''
+===CRYSTAL STRUCTURE OF AN ENGINEERED UROCANASE TETRAMER===
-==Overview==
+<!--
-The analysis of natural contact interfaces between protein subunits and between proteins has disclosed some general rules governing their association. We have applied these rules to produce a number of novel assemblies, demonstrating that a given protein can be engineered to form contacts at various points of its surface. Symmetry plays an important role because it defines the multiplicity of a designed contact and therefore the number of required mutations. Some of the proteins needed only a single side-chain alteration in order to associate to a higher-order complex. The mobility of the buried side chains has to be taken into account. Four assemblies have been structurally elucidated. Comparisons between the designed contacts and the results will provide useful guidelines for the development of future architectures.
+The line below this paragraph, {{ABSTRACT_PUBMED_18187656}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18187656 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18187656}}
 ==About this Structure==
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 [[Category: Protein engineering]]
 [[Category: Urocanate hydratase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 18:19:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:17:46 2008''