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.


1hzn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hzn.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1hzn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hzn| PDB=1hzn | SCENE= }}
{{STRUCTURE_1hzn| PDB=1hzn | SCENE= }}
-
'''NMR SOLUTION STRUCTURE OF THE THIRD EXTRACELLULAR LOOP OF THE CHOLECYSTOKININ A RECEPTOR'''
+
===NMR SOLUTION STRUCTURE OF THE THIRD EXTRACELLULAR LOOP OF THE CHOLECYSTOKININ A RECEPTOR===
-
==Overview==
+
<!--
-
The interaction of the C-terminal octapeptide of cholecystokinin, CCK-8, with the third extracellular loop of human cholecystokinin-A receptor, CCK(A)-R(329-357), has been probed by high-resolution NMR and extensive computer simulations. The structure of CCK(A)-R(329-357) in the presence of dodecylphosphocholine micelles consists of three alpha-helices, with the first and third corresponding to the extracellular ends of transmembrane (TM) helices 6 and 7. The central helix, residues W335-R345, is found to lie on the zwitterionic surface. Titration with CCK-8 produces a stable complex with a number of intermolecular NOEs between the C-terminus of the ligand (Trp(30), Met(31), Asp(32)) and the interface of TM6 and the third extracellular loop (N333, A334, Y338) of the receptor fragment. The mode of ligand binding based on these intermolecular NOEs is in agreement with a number of published findings from receptor mutagenesis and photoaffinity cross-linking. Utilizing these ligand/receptor points of interaction, the structural features of CCK(A)-R(329-357), and also the structures of CCK-8 and CCK(A)-R(1-47) previously determined, extensive molecular dynamics simulations of the CCK-8/CCK(A)-R complex were carried out. The results provide unique insight into the molecular interactions and forces important for the binding of CCK-8 to CCK(A)-R.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11300760}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11300760 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11300760}}
==About this Structure==
==About this Structure==
-
1HZN is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZN OCA].
+
1HZN is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZN OCA].
==Reference==
==Reference==
Line 24: Line 28:
[[Category: Mierke, D F.]]
[[Category: Mierke, D F.]]
[[Category: Hormone/growth factor]]
[[Category: Hormone/growth factor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:24:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:11:22 2008''

Revision as of 07:11, 1 July 2008

Image:1hzn.png

Template:STRUCTURE 1hzn

NMR SOLUTION STRUCTURE OF THE THIRD EXTRACELLULAR LOOP OF THE CHOLECYSTOKININ A RECEPTOR

Template:ABSTRACT PUBMED 11300760

About this Structure

1HZN is a Single protein structure. Full experimental information is available from OCA.

Reference

Intermolecular interactions between cholecystokinin-8 and the third extracellular loop of the cholecystokinin A receptor., Giragossian C, Mierke DF, Biochemistry. 2001 Apr 3;40(13):3804-9. PMID:11300760

Page seeded by OCA on Tue Jul 1 10:11:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hzn"
Personal tools