Designed Protein-Protein Association

by: Dirk Grueninger, Nora Treiber, Mathias O Ziegler, Jochen W Koetter, Monika-Sarah Schulze, Georg E Schulz

Science, Vol. 319, No. 5860. (11 January 2008), pp. 206-209.

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Abstract

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. 10.1126/science.1150421

@article{citeulike:2220255, abstract = {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. 10.1126/science.1150421}, author = {Grueninger, Dirk and Treiber, Nora and Ziegler, Mathias O. and Koetter, Jochen W. and Schulze, Monika-Sarah and Schulz, Georg E. }, citeulike-article-id = {2220255}, doi = {10.1126/science.1150421}, journal = {Science}, keywords = {clip2, design, mutation, oligomer, protein}, month = {January}, number = {5860}, pages = {206--209}, posted-at = {2008-01-15 06:10:38}, priority = {2}, title = {Designed Protein-Protein Association}, url = {http://dx.doi.org/10.1126/science.1150421}, volume = {319}, year = {2008} }

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TY - JOUR ID - citeulike:2220255 L3 - citeulike-article-id:2220255 TI - Designed Protein-Protein Association JF - Science VL - 319 IS - 5860 SP - 206 EP - 209 N2 - 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. 10.1126/science.1150421 KW - clip2 KW - design KW - mutation KW - oligomer KW - protein AU - Grueninger, Dirk AU - Treiber, Nora AU - Ziegler, Mathias AU - Koetter, Jochen AU - Schulze, Monika-Sarah AU - Schulz, Georg PY - 2008/01/11/ UR - http://dx.doi.org/10.1126/science.1150421 ER -

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