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Intrinsic motions in the N-terminal domain of an ionotropic glutamate receptor detected by fluorescence correlation spectroscopy.

Abstract：

:Ionotropic glutamate receptors (iGluRs) mediate excitatory neurotransmission in the central nervous system and play key roles in brain development and disease. iGluRs have two distinct extracellular domains, but the functional role of the distal N-terminal domain (NTD) is poorly understood. Crystal structures of the NTD from some non-N-methyl-d-aspartate (NMDA) iGluRs are consistent with a rigid body that facilitates receptor assembly but suggest an additional dynamic role that could modulate signaling. Here, we moved beyond spatial and temporal limitations of conventional protein single-molecule spectroscopy by employing correlation analysis of extrinsic oxazine fluorescence fluctuations. We observed nanosecond (ns)-to-microsecond (μs) motions of loop segments and helices within a region of an AMPA-type iGluR NTD, which has been identified previously to be structurally variable. Our data reveal that the AMPA receptor NTD undergoes rapid conformational fluctuations, suggesting an inherent allosteric capacity for this domain in addition to its established assembly function.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Jensen MH,Sukumaran M,Johnson CM,Greger IH,Neuweiler H

doi

10.1016/j.jmb.2011.09.037

subject

Has Abstract

pub_date

2011-11-18 00:00:00

pages

96-105

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(11)01077-1

journal_volume

414

pub_type

杂志文章

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