This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1d6g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 1d6g |SIZE=350|CAPTION= <scene name='initialview01'>1d6g</scene>
|PDB= 1d6g |SIZE=350|CAPTION= <scene name='initialview01'>1d6g</scene>
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene>
+
|LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d6g OCA], [http://www.ebi.ac.uk/pdbsum/1d6g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d6g RCSB]</span>
}}
}}
Line 23: Line 26:
[[Category: Mierke, D F.]]
[[Category: Mierke, D F.]]
[[Category: Pellegrini, M.]]
[[Category: Pellegrini, M.]]
-
[[Category: NH2]]
 
[[Category: alpha-helix]]
[[Category: alpha-helix]]
[[Category: beta-sheet]]
[[Category: beta-sheet]]
[[Category: complex gpcr-ligand]]
[[Category: complex gpcr-ligand]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:33:32 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:35:44 2008''

Revision as of 16:35, 30 March 2008


PDB ID 1d6g

Drag the structure with the mouse to rotate
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
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

Page seeded by OCA on Sun Mar 30 19:35:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools