Kinetic contributions to gating by interactions unique to N-methyl-D-aspartate (NMDA) receptors

William F. Borschel; Kirstie A. Cummings; Leeann K. Tindell; Gabriela K. Popescu

doi:10.1074/jbc.M115.678656

Kinetic contributions to gating by interactions unique to N-methyl-D-aspartate (NMDA) receptors

William F. Borschel
, Kirstie A. Cummings
, Leeann K. Tindell
, Gabriela K. Popescu

Biochemistry

SUNY Buffalo

Research output: Contribution to journal › Article › peer-review

23 Scopus citations

Abstract

Background: NMDA receptor deactivation is characteristically slow and depends on unique intersubunit contacts in the ligand binding domain. Results: These additional contacts slow current deactivation mainly by increasing gating. Conclusion: Slow deactivation reflects higher open probability due to more stable heterodimers. Significance: A firmer heterodimer interface supports basic functional differences between NMDA and non-NMDA glutamate-gated channels.

Original language	English
Pages (from-to)	26846-26855
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	290
Issue number	44
DOIs	https://doi.org/10.1074/jbc.M115.678656
State	Published - Oct 30 2015

Access to Document

10.1074/jbc.M115.678656

Cite this

@article{e88507c3cac04ccf8956bf06b0e78267,

title = "Kinetic contributions to gating by interactions unique to N-methyl-D-aspartate (NMDA) receptors",

abstract = "Background: NMDA receptor deactivation is characteristically slow and depends on unique intersubunit contacts in the ligand binding domain. Results: These additional contacts slow current deactivation mainly by increasing gating. Conclusion: Slow deactivation reflects higher open probability due to more stable heterodimers. Significance: A firmer heterodimer interface supports basic functional differences between NMDA and non-NMDA glutamate-gated channels.",

author = "Borschel, \{William F.\} and Cummings, \{Kirstie A.\} and Tindell, \{Leeann K.\} and Popescu, \{Gabriela K.\}",

note = "Publisher Copyright: {\textcopyright} 2015 by The American Society for Biochemistry and Molecular Biology, Inc.",

year = "2015",

month = oct,

day = "30",

doi = "10.1074/jbc.M115.678656",

language = "English",

volume = "290",

pages = "26846--26855",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "44",

}

TY - JOUR

T1 - Kinetic contributions to gating by interactions unique to N-methyl-D-aspartate (NMDA) receptors

AU - Borschel, William F.

AU - Cummings, Kirstie A.

AU - Tindell, Leeann K.

AU - Popescu, Gabriela K.

PY - 2015/10/30

Y1 - 2015/10/30

N2 - Background: NMDA receptor deactivation is characteristically slow and depends on unique intersubunit contacts in the ligand binding domain. Results: These additional contacts slow current deactivation mainly by increasing gating. Conclusion: Slow deactivation reflects higher open probability due to more stable heterodimers. Significance: A firmer heterodimer interface supports basic functional differences between NMDA and non-NMDA glutamate-gated channels.

AB - Background: NMDA receptor deactivation is characteristically slow and depends on unique intersubunit contacts in the ligand binding domain. Results: These additional contacts slow current deactivation mainly by increasing gating. Conclusion: Slow deactivation reflects higher open probability due to more stable heterodimers. Significance: A firmer heterodimer interface supports basic functional differences between NMDA and non-NMDA glutamate-gated channels.

UR - https://www.scopus.com/pages/publications/84946042670

U2 - 10.1074/jbc.M115.678656

DO - 10.1074/jbc.M115.678656

M3 - Article

C2 - 26370091

AN - SCOPUS:84946042670

SN - 0021-9258

VL - 290

SP - 26846

EP - 26855

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 44

ER -

Kinetic contributions to gating by interactions unique to N-methyl-D-aspartate (NMDA) receptors

Abstract

Access to Document

Other files and links

Fingerprint

Cite this