NDLI: Use of Multidimensional Fluorescence Resonance Energy Transfer To Establish the Orientation of Cholecystokinin Docked at the Type A Cholecystokinin Receptor †

Content Provider	PubMed Central
Author	Harikumar, Kaleeckal G. Gao, Fan Pinon, Delia I. Miller, Laurence J.
Copyright Year	2008
Abstract	Fluorescence resonance energy transfer (FRET) represents a powerful tool to establish relative distances between donor and acceptor fluorophores. By utilizing several donors situated in distinct positions within a docked full agonist ligand and several acceptors distributed at distinct sites within its receptor, multiple interdependent dimensions can be determined. These can provide a unique method to establish or confirm three-dimensional structure of the molecular complex. In this work, we have utilized full agonist analogues of cholecystokinin (CCK) with Aladan distributed throughout the pharmacophore in positions 24, 29, and 33, along with receptor constructs derivatized with Alexa546 at positions 94, 102, 204, and 341 in the helical bundle and first, second, and third extracellular loops, respectively. These provided 12 FRET distances to overlay on working models of the CCK-occupied receptor. These established that the carboxyl terminus of CCK resides at the external surface of the lipid bilayer, adjacent to the receptor amino-terminal tail, rather than being inserted into the helical bundle. They also provide important experimentally derived constraints for understanding spatial relationships between the docked ligand and the flexible extracellular loop regions. Multidimensional FRET provides a new independent method to establish and refine structural insights into ligand–receptor complexes.
Related Links	http://dx.doi.org/10.1021/bi800734w
Ending Page	9581
Page Count	8
Starting Page	9574
File Format	PDF
ISSN	00062960
e-ISSN	15204995
Journal	Biochemistry
Issue Number	36
Volume Number	47
Language	English
Publisher Date	2008-09-09
Access Restriction	Open
Subject Keyword	Biochemistry Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry

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