Recognition Pliability Is Coupled to Structural Heterogeneity: A Calmodulin Intrinsically Disordered Binding Region Complex (Journal article)

Nagulapalli, M./ Parigi, G./ Yuan, J./ Gsponer, J./ Deraos, G./ Bamm, V. V./ Harauz, G./ Matsoukas, J./ de Planque, M. R. R./ Gerothanassis, I. P./ Babu, M. M./ Luchinat, C./ Tzakos, A. G.

Protein interactions within regulatory networks should adapt in a spatiotemporal-dependent dynamic environment, in order to process and respond to diverse and versatile cellular signals. However, the principles governing recognition pliability in protein complexes are not well understood. We have investigated a region of the intrinsically disordered protein myelin basic protein (MBP145-165) that interacts with calmodulin, but that also promiscuously binds other biomolecules (membranes, modifying enzymes). To characterize this interaction, we implemented an NMR spectroscopic approach that calculates, for each conformation of the complex, the maximum occurrence based on recorded pseudocontact shifts and residual dipolar couplings. We found that the MBP145-165-calmodulin interaction is characterized by structural heterogeneity. Quantitative comparative analysis indicated that distinct conformational landscapes of structural heterogeneity are sampled for different calmodulin-target complexes. Such structural heterogeneity in protein complexes could potentially explain the way that transient and promiscuous protein interactions are optimized and tuned in complex regulatory networks.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας
Keywords: myelin basic-protein,nmr-spectroscopy,unstructured proteins,molecular recognition,conformational space,multiple-sclerosis,target recognition,backbone dynamics,fuzzy complexes,human-diseases
ISSN: 0969-2126
Link: <Go to ISI>://000301328800018
Publisher: Elsevier
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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