A conserved GXXXG motif in the transmembrane domain of CLIC proteins is essential for their cholesterol-dependant membrane interaction

2019 ◽  
Vol 1863 (8) ◽  
pp. 1243-1253 ◽  
Author(s):  
Khondker Rufaka Hossain ◽  
Daniel R. Turkewitz ◽  
Stephen A. Holt ◽  
Leonie Herson ◽  
Louise J. Brown ◽  
...  
Keyword(s):  
Transmembrane Domain ◽  
Membrane Interaction ◽  
Gxxxg Motif

Complex Patterns of Histidine, Hydroxylated Amino Acids and the GxxxG Motif Mediate High-affinity Transmembrane Domain Interactions

2009 ◽  
Vol 385 (3) ◽  
pp. 912-923 ◽  
Author(s):  
Jana R. Herrmann ◽  
Johanna C. Panitz ◽  
Stephanie Unterreitmeier ◽  
Angelika Fuchs ◽  
Dmitrij Frishman ◽  
...  
Keyword(s):  
Amino Acids ◽  
Transmembrane Domain ◽  
High Affinity ◽  
Gxxxg Motif ◽  
Domain Interactions ◽  
Complex Patterns

scholarly journals Differential Transmembrane Domain GXXXG Motif Pairing Impacts Major Histocompatibility Complex (MHC) Class II Structure

2014 ◽  
Vol 289 (17) ◽  
pp. 11695-11703 ◽  
Author(s):  
Ann M. Dixon ◽  
Lisa Drake ◽  
Kelly T. Hughes ◽  
Elizabeth Sargent ◽  
Danielle Hunt ◽  
...  
Keyword(s):  
Major Histocompatibility Complex ◽  
Mhc Class Ii ◽  
Transmembrane Domain ◽  
Class Ii ◽  
Major Histocompatibility ◽  
Histocompatibility Complex ◽  
Gxxxg Motif

A Trimerizing GxxxG Motif Is Uniquely Inserted in the Severe Acute Respiratory Syndrome (SARS) Coronavirus Spike Protein Transmembrane Domain†

Biochemistry ◽  
2006 ◽  
Vol 45 (38) ◽  
pp. 11349-11356 ◽  
Author(s):  
Eyal Arbely ◽  
Zvi Granot ◽  
Itamar Kass ◽  
Joseph Orly ◽  
Isaiah T. Arkin
Keyword(s):  
Severe Acute Respiratory Syndrome ◽  
Transmembrane Domain ◽  
Spike Protein ◽  
Sars Coronavirus ◽  
Gxxxg Motif

scholarly journals Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex

BMC Biology ◽  
2008 ◽  
Vol 6 (1) ◽  
Author(s):  
Ding-Kwo Chang ◽  
Shu-Fang Cheng ◽  
Eric Aseen B Kantchev ◽  
Chi-Hui Lin ◽  
Yu-Tsan Liu
Keyword(s):  
Transmembrane Domain ◽  
Fusion Peptide ◽  
Membrane Interaction ◽  
Peptide Complex ◽  
Influenza Hemagglutinin

scholarly journals GxxxG Motif of Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein Transmembrane Domain Is Not Involved in Trimerization and Is Not Important for Entry

2007 ◽  
Vol 81 (15) ◽  
pp. 8352-8355 ◽  
Author(s):  
Jeroen Corver ◽  
Rene Broer ◽  
Puck van Kasteren ◽  
Willy Spaan
Keyword(s):  
Severe Acute Respiratory Syndrome ◽  
Transmembrane Domain ◽  
Vital Role ◽  
Sars Coronavirus ◽  
Spike Glycoprotein ◽  
S Protein ◽  
Mutant Proteins ◽  
Gxxxg Motif

ABSTRACT Recently, a paper was published in which it was proposed that the GxxxG motif of the severe acute respiratory syndrome (SARS) coronavirus spike (S) protein transmembrane domain plays a vital role in oligomerization of the protein (E. Arbely, Z. Granot, I. Kass, J. Orly, and I. T. Arkin, Biochemistry 45:11349-11356, 2006). Here, we show that the GxxxG motif is not involved in SARS S oligomerization by trimerization analysis of S GxxxG mutant proteins. In addition, the capability of S to mediate entry of SARS S-pseudotyped particles overall was affected moderately in the mutant proteins, also arguing for a nonvital role for the GxxxG motif in SARS coronavirus entry.

The GxxxG motif of the transmembrane domain of subunit e is involved in the dimerization/oligomerization of the yeast ATP synthase complex in the mitochondrial membrane

2003 ◽  
Vol 270 (8) ◽  
pp. 1875-1884 ◽  
Author(s):  
Genevieve Arselin ◽  
Marie-France Giraud ◽  
Alain Dautant ◽  
Jacques Vaillier ◽  
Daniel Brethes ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Mitochondrial Membrane ◽  
Transmembrane Domain ◽  
Gxxxg Motif ◽  
Subunit E
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