1d6g
From Proteopedia
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| - | [[Image:1d6g.gif|left|200px]] | + | [[Image:1d6g.gif|left|200px]] |
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| - | '''MOLECULAR COMPLEX OF CHOLECYSTOKININ-8 AND N-TERMINUS OF THE CHOLECYSTOKININ A RECEPTOR BY NMR SPECTROSCOPY''' | + | {{Structure |
| + | |PDB= 1d6g |SIZE=350|CAPTION= <scene name='initialview01'>1d6g</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''MOLECULAR COMPLEX OF CHOLECYSTOKININ-8 AND N-TERMINUS OF THE CHOLECYSTOKININ A RECEPTOR BY NMR SPECTROSCOPY''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1D6G is a [ | + | 1D6G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D6G OCA]. |
==Reference== | ==Reference== | ||
| - | Molecular complex of cholecystokinin-8 and N-terminus of the cholecystokinin A receptor by NMR spectroscopy., Pellegrini M, Mierke DF, Biochemistry. 1999 Nov 9;38(45):14775-83. PMID:[http:// | + | Molecular complex of cholecystokinin-8 and N-terminus of the cholecystokinin A receptor by NMR spectroscopy., Pellegrini M, Mierke DF, Biochemistry. 1999 Nov 9;38(45):14775-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10555959 10555959] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Mierke, D F.]] | [[Category: Mierke, D F.]] | ||
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[[Category: complex gpcr-ligand]] | [[Category: complex gpcr-ligand]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:33:32 2008'' |
Revision as of 08:33, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
MOLECULAR COMPLEX OF CHOLECYSTOKININ-8 AND N-TERMINUS OF THE CHOLECYSTOKININ A RECEPTOR BY NMR SPECTROSCOPY
Overview
The bimolecular complex of the C-terminal octapeptide of cholecystokinin, CCK-8, with the N-terminus of the CCK(A)-receptor, CCK(A)-R(1-47), has been structurally characterized by high-resolution NMR and computational refinement. The conformation of CCK(A)-R(1-47), within the lipid environment used for the spectroscopic studies, consists of a well-defined alpha-helix (residues 3-9) followed by a beta-sheet stabilized by a disulfide linkage between C18 and C29, leading to the first transmembrane alpha-helix (TM1). Titration of CCK(A)-R(1-47) with CCK-8 specifically affects the NMR signals of W39 of the receptor, in a saturable fashion. This association is specific for CCK-8; no association was observed upon titration of CCK(A)-R(1-47) with other peptide hormones. The ligand/receptor complex was characterized by intermolecular NOEs between Tyr(27) and Met(28) of CCK-8 and W39 of CCK(A)-R(1-47). These findings suggest that CCK-8 binds to CCK(A) with the C-terminus within the seven-helical bundle and the N-terminus of the ligand, projecting out between TM1 and TM7, forming specific interactions with the N-terminus of the CCK(A) receptor. This mode of ligand binding, consistent with published mutagenesis studies, requires variation of the interpretation of recent findings from photoaffinity cross-linking studies.
About this Structure
1D6G is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Molecular complex of cholecystokinin-8 and N-terminus of the cholecystokinin A receptor by NMR spectroscopy., Pellegrini M, Mierke DF, Biochemistry. 1999 Nov 9;38(45):14775-83. PMID:10555959
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