1l4t
From Proteopedia
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[[Image:1l4t.gif|left|200px]] | [[Image:1l4t.gif|left|200px]] | ||
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| - | | | + | {{STRUCTURE_1l4t| PDB=1l4t | SCENE= }} |
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'''SOLUTION NMR STRUCTURE OF THE CCK2E3''' | '''SOLUTION NMR STRUCTURE OF THE CCK2E3''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L4T is a [[Single protein]] structure | + | 1L4T is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4T OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Giragossian, C.]] | [[Category: Giragossian, C.]] | ||
[[Category: Mierke, D F.]] | [[Category: Mierke, D F.]] | ||
| - | [[Category: | + | [[Category: Hormone/growth factor receptor]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:32:21 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:32, 2 May 2008
SOLUTION NMR STRUCTURE OF THE CCK2E3
Overview
The structure of the third extracellular loop of the human cholecystokinin-2 receptor, CCK2-R(352-379), and its interactions with the C-terminal octapeptide of cholecystokinin (CCK-8) have been determined by high-resolution NMR and computer simulations. In the presence of dodecylphosphocholine micelles, the structure of the receptor fragment consisted of three helices, with the first and third corresponding to residues of the extracellular ends of transmembrane helices (TM) 6 and 7, respectively. The central, extracellular helix, consisting of residues 363-368, was found to be closely associated with the membrane mimetic used during the spectroscopic studies and molecular dynamics (MD) simulations. Upon titration of CCK-8 to the receptor domain, chemical shift perturbation and intermolecular NOEs (Trp30, Met31 of CCK-8 and P371, F374 of CCK2-R) indicated the formation of a stable complex and specific ligand/receptor interactions. Using the NOE-generated intermolecular contact points, extensive MD simulations of CCK-8 bound to the CCK2 receptor were carried out. The results, with CCK-8 in close proximity to TM7, differ from previous structural studies of CCK-8 association with CCK1-R, in which the ligand formed a number of interactions with TM6. These differences may play a role in the ligand specificity displayed by the CCK1 and CCK2 receptor subtypes.
About this Structure
1L4T is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Intermolecular interactions between cholecystokinin-8 and the third extracellular loop of the cholecystokinin-2 receptor., Giragossian C, Mierke DF, Biochemistry. 2002 Apr 9;41(14):4560-6. PMID:11926817 Page seeded by OCA on Fri May 2 23:32:21 2008
