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.


1sa4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1sa4.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1sa4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sa4| PDB=1sa4 | SCENE= }}
{{STRUCTURE_1sa4| PDB=1sa4 | SCENE= }}
-
'''human protein farnesyltransferase complexed with FPP and R115777'''
+
===human protein farnesyltransferase complexed with FPP and R115777===
-
==Overview==
+
<!--
-
The search for new cancer therapeutics has identified protein farnesyltransferase (FTase) as a promising drug target. This enzyme attaches isoprenoid lipids to signal transduction proteins involved in growth and differentiation. The two FTase inhibitors (FTIs), R115777 (tipifarnib/Zarnestra) and BMS-214662, have undergone evaluation as cancer therapeutics in phase I and II clinical trials. R115777 has been evaluated in phase III clinical trials and shows indications for the treatment of blood and breast malignancies. Here we present crystal structures of R115777 and BMS-214662 complexed with mammalian FTase. These structures illustrate the molecular mechanism of inhibition and selectivity toward FTase over the related enzyme, protein geranylgeranyltransferase type I (GGTase-I). These results, combined with previous biochemical and structural analyses, identify features of FTase that could be exploited to modulate inhibitor potency and specificity and should aid in the continued development of FTIs as therapeutics for the treatment of cancer and parasitic infections.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15170324}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15170324 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15170324}}
==About this Structure==
==About this Structure==
Line 40: Line 44:
[[Category: Tumor regression]]
[[Category: Tumor regression]]
[[Category: Zarnestra]]
[[Category: Zarnestra]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:28:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:17:55 2008''

Revision as of 09:18, 27 July 2008

Image:1sa4.png

Template:STRUCTURE 1sa4

human protein farnesyltransferase complexed with FPP and R115777

Template:ABSTRACT PUBMED 15170324

About this Structure

1SA4 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structures of the anticancer clinical candidates R115777 (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase suggest a mechanism of FTI selectivity., Reid TS, Beese LS, Biochemistry. 2004 Jun 8;43(22):6877-84. PMID:15170324

Page seeded by OCA on Sun Jul 27 12:17:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sa4"
Personal tools