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Closing the Ring: A Fourth Extracellular Loop in Chemokine Receptors
Szpakowska, Martyna; Perez Bercoff, Danielle; Chevigné, Andy
2014In Science Signaling, 7 (34)
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Abstract :
[en] Chemokine receptors are heterotrimeric guanine nucleotide binding protein (G protein) coupled receptors (GPCR) that play fundamental roles in many physio- logical and pathological processes. Typically, these receptors form a seven-trans- membrane helix bundle, which is stabilized by a disulfi de bond bridging the top of the third transmembrane segment (TM3) and the second extracellular loop (ECL2). Resolution of the three-dimensional structures of the chemokine receptors CXCR1, CXCR4, and CCR5 revealed the existence of a second disulfi de bridge that links the N terminus of the receptor to the top of the seventh transmembrane segment (TM7), thereby closing the receptor into a ring. An important consequence of this second disulfi de bond is the formation of an additional extracellular loop, which shapes the entrance of the ligand-binding pocket and adds rigidity to the overall surface of the receptor. Here, we discuss the features of these pseudo-loops, the structural re- quirements for their formation, and the effects they may have on receptor function
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Szpakowska, Martyna ;  Université de Liège - ULiège > Doct. sc. (bioch., biol. mol.&cell., bioinf.&mod.-Bologne)
Perez Bercoff, Danielle
Chevigné, Andy
Language :
English
Title :
Closing the Ring: A Fourth Extracellular Loop in Chemokine Receptors
Publication date :
September 2014
Journal title :
Science Signaling
ISSN :
1945-0877
eISSN :
1937-9145
Publisher :
American Association for the Advancement of Science, Washington, United States - District of Columbia
Volume :
7
Issue :
34
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 12 June 2015

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