PMID- 11705385
OWN - NLM
STAT- MEDLINE
DCOM- 20011207
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 40
IP  - 46
DP  - 2001 Nov 20
TI  - First images of a glutamate receptor ion channel: oligomeric state and molecular 
      dimensions of GluRB homomers.
PG  - 13948-53
AB  - We have expressed, purified, and characterized glutamate receptor ion channels 
      (GluR) assembled as homomers of the subunit GluRB. For the first time, 
      single-milligram quantities of biochemically homogeneous GluR have been obtained. 
      The protein exhibits the expected pharmacological profile and a high specific 
      activity for ligand binding. Density-gradient centrifugation reveals a uniform 
      oligomeric assembly and a molecular mass suggesting that the channel is a 
      tetramer. On the basis of electron microscopic images, the receptor appears to 
      form an elongated structure that is visualized in several orientations. The 
      molecular dimensions of the molecule are approximately 11 x 14 x 17 nm, and 
      solvent-accessible features can be seen; these may contribute to formation of the 
      ion-conducting pathway of the channel. The channel dimensions are consistent with 
      an overall 2-fold symmetric assembly, suggesting that the tetrameric receptor may 
      be a dimer of dimers.
FAU - Safferling, M
AU  - Safferling M
AD  - Ion Channel Structure Research Group, Max Planck Institute for Medical Research, 
      Jahnstrasse 29, 69120 Heidelberg, Germany.
FAU - Tichelaar, W
AU  - Tichelaar W
FAU - Kummerle, G
AU  - Kummerle G
FAU - Jouppila, A
AU  - Jouppila A
FAU - Kuusinen, A
AU  - Kuusinen A
FAU - Keinanen, K
AU  - Keinanen K
FAU - Madden, D R
AU  - Madden DR
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Ion Channels)
RN  - 0 (Ligands)
RN  - 0 (Receptors, AMPA)
RN  - 0 (Recombinant Proteins)
RN  - 0 (glutamate receptor type B)
SB  - IM
MH  - Animals
MH  - Cells, Cultured
MH  - Centrifugation, Density Gradient
MH  - Ion Channels/*chemistry/genetics/isolation & purification/ultrastructure
MH  - Kinetics
MH  - Ligands
MH  - Microscopy, Electron
MH  - Rats
MH  - Receptors, AMPA/*chemistry/genetics/isolation & purification/ultrastructure
MH  - Recombinant Proteins/biosynthesis/chemistry/isolation & 
      purification/ultrastructure
MH  - Spodoptera/genetics
EDAT- 2001/11/14 10:00
MHDA- 2002/01/05 10:01
CRDT- 2001/11/14 10:00
PHST- 2001/11/14 10:00 [pubmed]
PHST- 2002/01/05 10:01 [medline]
PHST- 2001/11/14 10:00 [entrez]
AID - bi011143g [pii]
AID - 10.1021/bi011143g [doi]
PST - ppublish
SO  - Biochemistry. 2001 Nov 20;40(46):13948-53. doi: 10.1021/bi011143g.