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.


2fke

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2fke.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2fke.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2fke| PDB=2fke | SCENE= }}
{{STRUCTURE_2fke| PDB=2fke | SCENE= }}
-
'''FK-506-BINDING PROTEIN: THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX WITH THE ANTAGONIST L-685,818'''
+
===FK-506-BINDING PROTEIN: THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX WITH THE ANTAGONIST L-685,818===
-
==Overview==
+
<!--
-
L-685,818 differs only slightly in structure from the immunosuppressive drug FK-506, and both compounds bind with comparable affinity to the 12-kDa FK-506-binding protein (FKBP12), the major intracellular receptor for the drug. Despite these similarities, L-685,818 is a potent antagonist of both the immunosuppressive and toxic effects of the drug. Here, we present a structural analysis of this problem. Although FK-506 and L-685,818 differ greatly in pharmacology, we have found that the three-dimensional structures of their complexes with FKBP12 are essentially identical. Approximately half of each ligand is in contact with the receptor protein, and half is exposed to solvent; the exposed region includes the two sites where the compounds differ. These results indicate that the profound differences in the pharmacology of these two compounds are not caused by any difference in their interaction with FKBP12. Rather, these effects arise because relatively minor changes in the exposed part of a bound ligand have a strong effect on how FKBP12-ligand complexes interact with calcineurin, their putative intracellular target. In addition, FK-506 complexes with FKBP12 proteins from several species all inhibit mammalian calcineurin. Analysis of the three-dimensional structure of the complex with respect to residues conserved among these proteins suggests a small number of surface residues near the bound ligands that may play a critical role in interactions between the protein-drug complex and calcineurin.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7684380}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7684380 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7684380}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Rotonda, J.]]
[[Category: Rotonda, J.]]
[[Category: Cis-trans isomerase]]
[[Category: Cis-trans isomerase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:59:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:16:40 2008''

Revision as of 15:16, 27 July 2008

Image:2fke.png

Template:STRUCTURE 2fke

FK-506-BINDING PROTEIN: THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX WITH THE ANTAGONIST L-685,818

Template:ABSTRACT PUBMED 7684380

About this Structure

2FKE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

FK-506-binding protein: three-dimensional structure of the complex with the antagonist L-685,818., Becker JW, Rotonda J, McKeever BM, Chan HK, Marcy AI, Wiederrecht G, Hermes JD, Springer JP, J Biol Chem. 1993 May 25;268(15):11335-9. PMID:7684380

Page seeded by OCA on Sun Jul 27 18:16:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fke"
Personal tools