NDLI: Weak conservation of structural features in the interfaces of homologous transient protein-protein complexes.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Swapna, Lakshmipuram S. Srinivasan, Narayanaswamy Sudha, Govindarajan Singh, Prashant
Description	Country affiliation: India Author Affiliation: Sudha G ( Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560012, Karnataka, India.); Singh P ( Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560012, Karnataka, India.); Swapna LS ( Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560012, Karnataka, India.); Srinivasan N ( Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560012, Karnataka, India.)
Abstract	Residue types at the interface of protein-protein complexes (PPCs) are known to be reasonably well conserved. However, we show, using a dataset of known 3-D structures of homologous transient PPCs, that the 3-D location of interfacial residues and their interaction patterns are only moderately and poorly conserved, respectively. Another surprising observation is that a residue at the interface that is conserved is not necessarily in the interface in the homolog. Such differences in homologous complexes are manifested by substitution of the residues that are spatially proximal to the conserved residue and structural differences at the interfaces as well as differences in spatial orientations of the interacting proteins. Conservation of interface location and the interaction pattern at the core of the interfaces is higher than at the periphery of the interface patch. Extents of variability of various structural features reported here for homologous transient PPCs are higher than the variation in homologous permanent homomers. Our findings suggest that straightforward extrapolation of interfacial nature and inter-residue interaction patterns from template to target could lead to serious errors in the modeled complex structure. Understanding the evolution of interfaces provides insights to improve comparative modeling of PPC structures.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	11
Volume Number	24
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2015-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Binding Sites Multiprotein Complexes Chemistry Metabolism Protein Binding Models, Molecular Protein Conformation Structural Homology, Protein Surface Properties Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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