ReviewInteraction and conformational dynamics of membrane-spanning protein helices |
| Dieter Langosch 1 2 *, Isaiah T. Arkin 3 |
1Lehrstuhl Chemie der Biopolymere, Technische Universität München, Weihenstephaner Berg 3, 85354 Freising, Germany
2Munich Center for Integrated Protein Science (CIPSM), Munich, Germany
3Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem 91904, Israel
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| email: Dieter Langosch (langosch@lrz.tum.de) |
*Correspondence to Dieter Langosch, Lehrstuhl der Chemie der Biopolymere, Technische Universität München, Weihenstephaner Berg 3, 85354 Freising, Germany
Funded by:
Deutsche Forschungsgemeinschaft; Grant Number: La699/8-1,2,3, La699/9-1,2
Israeli Science Foundation; Grant Number: 784/01, 1249/05, 1581/08
The Volkswagen Foundation
The Munich Center for Integrative Protein Sciences (CIPSM)
The State of Bavaria
| transmembrane helix dynamics interaction assembly membrane protein |
Within 1 or 2 decades, the reputation of membrane-spanning  -helices has changed dramatically. Once mostly regarded as dull membrane anchors, transmembrane domains are now recognized as major instigators of protein-protein interaction. These interactions may be of exquisite specificity in mediating assembly of stable membrane protein complexes from cognate subunits. Further, they can be reversible and regulatable by external factors to allow for dynamic changes of protein conformation in biological function. Finally, these helices are increasingly regarded as dynamic domains. These domains can move relative to each other in different functional protein conformations. In addition, small-scale backbone fluctuations may affect their function and their impact on surrounding lipid shells. Elucidating the ways by which these intricate structural features are encoded by the amino acid sequences will be a fascinating subject of research for years to come. |
Received: 16 February 2009; Revised: 19 April 2009; Accepted: 20 April 2009
10.1002/pro.154
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