Structural features and interactions between transmembrane and juxtamembrane domains in membrane proteins

Reconstitution environment plays an important role in structural determination of membrane proteins. The present study explores this theme in two systems: (1) the TM domain of integrin αL/β2, a single-pass integral membrane protein that heterodimerizes in α/β pairs, and (2) CoV E protein, a single-p...

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Main Author: Surya, Wahyu
Other Authors: Jaume Torres
Format: Thesis
Language:English
Published: 2017
Subjects:
Online Access:http://hdl.handle.net/10356/69964
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author Surya, Wahyu
author2 Jaume Torres
author_facet Jaume Torres
Surya, Wahyu
author_sort Surya, Wahyu
collection NTU
description Reconstitution environment plays an important role in structural determination of membrane proteins. The present study explores this theme in two systems: (1) the TM domain of integrin αL/β2, a single-pass integral membrane protein that heterodimerizes in α/β pairs, and (2) CoV E protein, a single-pass integral membrane protein that forms homopentameric ion channels. Monomeric and oligomeric structural models for integrin αL/β2 and E protein were determined by solution NMR. The model of αL/β2 TM heterodimer determined herein supports the "backbone reversal" structural feature previously observed only in αIIb/β3 TM in bicelles, instead of an α-helix observed in the presence of micelles or organic solvent. Yet, it is possible that the two forms reflect different activation states of integrin. Monomeric model for CoV E protein revealed conformational flexibility with functional relevance at the C-terminal extramembrane domain. The pentameric model offered possible explanations for the ion channel activity of E protein. In both systems, we found that the alternate forms observed under different reconstitution environment may reflect alternative conformation with functional relevance.
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spelling ntu-10356/699642023-02-28T18:46:37Z Structural features and interactions between transmembrane and juxtamembrane domains in membrane proteins Surya, Wahyu Jaume Torres School of Biological Sciences DRNTU::Science::Biological sciences::Biophysics Reconstitution environment plays an important role in structural determination of membrane proteins. The present study explores this theme in two systems: (1) the TM domain of integrin αL/β2, a single-pass integral membrane protein that heterodimerizes in α/β pairs, and (2) CoV E protein, a single-pass integral membrane protein that forms homopentameric ion channels. Monomeric and oligomeric structural models for integrin αL/β2 and E protein were determined by solution NMR. The model of αL/β2 TM heterodimer determined herein supports the "backbone reversal" structural feature previously observed only in αIIb/β3 TM in bicelles, instead of an α-helix observed in the presence of micelles or organic solvent. Yet, it is possible that the two forms reflect different activation states of integrin. Monomeric model for CoV E protein revealed conformational flexibility with functional relevance at the C-terminal extramembrane domain. The pentameric model offered possible explanations for the ion channel activity of E protein. In both systems, we found that the alternate forms observed under different reconstitution environment may reflect alternative conformation with functional relevance. ​Doctor of Philosophy (SBS) 2017-04-06T02:03:33Z 2017-04-06T02:03:33Z 2017 Thesis Surya, W. (2017). Structural features and interactions between transmembrane and juxtamembrane domains in membrane proteins. Doctoral thesis, Nanyang Technological University, Singapore. http://hdl.handle.net/10356/69964 10.32657/10356/69964 en 122 p. application/pdf
spellingShingle DRNTU::Science::Biological sciences::Biophysics
Surya, Wahyu
Structural features and interactions between transmembrane and juxtamembrane domains in membrane proteins
title Structural features and interactions between transmembrane and juxtamembrane domains in membrane proteins
title_full Structural features and interactions between transmembrane and juxtamembrane domains in membrane proteins
title_fullStr Structural features and interactions between transmembrane and juxtamembrane domains in membrane proteins
title_full_unstemmed Structural features and interactions between transmembrane and juxtamembrane domains in membrane proteins
title_short Structural features and interactions between transmembrane and juxtamembrane domains in membrane proteins
title_sort structural features and interactions between transmembrane and juxtamembrane domains in membrane proteins
topic DRNTU::Science::Biological sciences::Biophysics
url http://hdl.handle.net/10356/69964
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