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Recognition pliability is coupled to structural heterogeneity: a calmodulin intrinsically disordered binding region complex

Recognition pliability is coupled to structural heterogeneity: a calmodulin intrinsically disordered binding region complex
Recognition pliability is coupled to structural heterogeneity: a calmodulin intrinsically disordered binding region complex
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 (MBP(145-165)) 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 MBP(145-165)-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.
0969-2126
522-533
Nagulapalli, Malini
f97e7f91-0bf0-4822-b49c-f3221d525504
Parigi, Giacomo
6a9fcec1-9bcf-45a0-b41d-a7bd259151b0
Yuan, Jing
ca5fd83c-fea2-48e3-b1e8-361cd373e58c
Gsponer, Joerg
f82c1f48-fde2-463c-b9b3-9da89fc55d01
Deraos, George
f6416a74-30fb-4649-92e6-cf75ea2fd1db
Bamm, Vladimir V.
1a6906da-f72c-46b0-b135-6bc6efcfa2cd
Harauz, George
86d33766-0697-4cec-ac07-d312c4311702
Matsoukas, John
8062e4ca-b1ef-46b3-a5aa-8ae31b339a4c
de Planque, Maurits R.R.
a1d33d13-f516-44fb-8d2c-c51d18bc21ba
Gerothanassis, Ioannis P.
3f00d566-ada4-42b0-b0d9-3e60000450fc
Babu, M. Madan
5a0e2474-afeb-4f40-90bf-940147a603fe
Tzakos, Andreas G.
1af1bc7c-e2a9-4002-8a61-4fbe17becd80
Nagulapalli, Malini
f97e7f91-0bf0-4822-b49c-f3221d525504
Parigi, Giacomo
6a9fcec1-9bcf-45a0-b41d-a7bd259151b0
Yuan, Jing
ca5fd83c-fea2-48e3-b1e8-361cd373e58c
Gsponer, Joerg
f82c1f48-fde2-463c-b9b3-9da89fc55d01
Deraos, George
f6416a74-30fb-4649-92e6-cf75ea2fd1db
Bamm, Vladimir V.
1a6906da-f72c-46b0-b135-6bc6efcfa2cd
Harauz, George
86d33766-0697-4cec-ac07-d312c4311702
Matsoukas, John
8062e4ca-b1ef-46b3-a5aa-8ae31b339a4c
de Planque, Maurits R.R.
a1d33d13-f516-44fb-8d2c-c51d18bc21ba
Gerothanassis, Ioannis P.
3f00d566-ada4-42b0-b0d9-3e60000450fc
Babu, M. Madan
5a0e2474-afeb-4f40-90bf-940147a603fe
Tzakos, Andreas G.
1af1bc7c-e2a9-4002-8a61-4fbe17becd80

Nagulapalli, Malini, Parigi, Giacomo, Yuan, Jing, Gsponer, Joerg, Deraos, George, Bamm, Vladimir V., Harauz, George, Matsoukas, John, de Planque, Maurits R.R., Gerothanassis, Ioannis P., Babu, M. Madan and Tzakos, Andreas G. (2012) Recognition pliability is coupled to structural heterogeneity: a calmodulin intrinsically disordered binding region complex. Structure, 20 (3), 522-533. (doi:10.1016/j.str.2012.01.021). (PMID:22405011)

Record type: Article

Abstract

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 (MBP(145-165)) 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 MBP(145-165)-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.

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More information

Published date: 6 March 2012
Organisations: Nanoelectronics and Nanotechnology

Identifiers

Local EPrints ID: 344258
URI: https://eprints.soton.ac.uk/id/eprint/344258
ISSN: 0969-2126
PURE UUID: 8c5ee479-4bbe-4f9f-8fd5-e1e475c11365
ORCID for Maurits R.R. de Planque: ORCID iD orcid.org/0000-0002-8787-0513

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Date deposited: 15 Oct 2012 15:37
Last modified: 20 Jul 2019 00:51

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Contributors

Author: Malini Nagulapalli
Author: Giacomo Parigi
Author: Jing Yuan
Author: Joerg Gsponer
Author: George Deraos
Author: Vladimir V. Bamm
Author: George Harauz
Author: John Matsoukas
Author: Ioannis P. Gerothanassis
Author: M. Madan Babu
Author: Andreas G. Tzakos

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