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Understanding the role of domain-domain linkers in the spatial orientation of domains in multi-domain proteins

Bhaskara, Ramachandra M and de Brevern, Alexandre G and Srinivasan, Narayanaswamy (2013) Understanding the role of domain-domain linkers in the spatial orientation of domains in multi-domain proteins. In: JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 31 (12). pp. 1467-1480.

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Official URL: http://dx.doi.org/10.1080/07391102.2012.743438


Inter-domain linkers (IDLs)' bridge flanking domains and support inter-domain communication in multi-domain proteins. Their sequence and conformational preferences enable them to carry out varied functions. They also provide sufficient flexibility to facilitate domain motions and, in conjunction with the interacting interfaces, they also regulate the inter-domain geometry (IDG). In spite of the basic intuitive understanding of the inter-domain orientations with respect to linker conformations and interfaces, we still do not entirely understand the precise relationship among the three. We show that IDG is evolutionarily well conserved and is constrained by the domain-domain interface interactions. The IDLs modulate the interactions by varying their lengths, conformations and local structure, thereby affecting the overall IDG. Results of our analysis provide guidelines in modelling of multi-domain proteins from the tertiary structures of constituent domain components.

Item Type: Journal Article
Additional Information: Copyright for this article belongs to TAYLOR & FRANCIS INC USA
Keywords: multi-domain proteins; inter-domain linkers; inter-domain orientation; linker flexibility; interface constraints
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 06 Dec 2013 07:50
Last Modified: 06 Dec 2013 07:50
URI: http://eprints.iisc.ac.in/id/eprint/47882

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