University of Cambridge > Talks.cam > Experimental and Computational Aspects of Structural Biology and Applications to Drug Discovery > Domain swapping in proteins

Domain swapping in proteins

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  • UserDr Sowdhamini, National Centre for Biological Sciences (TIFR) UAS-GKVK Campus Bellary Road Bangalore 560 065 INDIA
  • ClockWednesday 21 December 2011, 10:15-11:15
  • HousePerham's seminar room.

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Structures of protein domains offer a dataset to understand the features that mediate their biological function. 3D domain swapping is a structural phenomenon observed in a variety of proteins as a mechanism for dimer or higher oligomeric formation. It is also implicated in neurodegenerative diseases since domain swapping could mediate unlimited oligomerisation. Data on all the available protein structural entries involved in this mechanism have been curated. Information on domain swapping has been obtained from the literature and bioinformatics tools and database resources and reported in a new database, “3Dswap”, for 293 non-redundant protein structures. We propose a quantitative method ‘extent of swapping’ to classify proteins involved in swapping mechanism and observed that large amount of proteins belong to the class of “moderately swapped” proteins. Structural entries from 3DSwap contribute to the ‘positive dataset’ and used for the development of machine learning-based approaches for the identification of sequence and structural features mediating 3D domain swapping. Support Vector Machine (SVM) and Random Forest (RF) based algorithms were developed to predict swapping from structure and mere sequence information. These prediction methods achieve 73% and 64% accuracy, respectively. I will also describe some structural analyses associated with these studies.

This talk is part of the Experimental and Computational Aspects of Structural Biology and Applications to Drug Discovery series.

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