We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1ft2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ft2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ft2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ft2| PDB=1ft2 | SCENE= }}
{{STRUCTURE_1ft2| PDB=1ft2 | SCENE= }}
-
'''CO-CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A FARNESYL DIPHOSPHATE SUBSTRATE'''
+
===CO-CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A FARNESYL DIPHOSPHATE SUBSTRATE===
-
==Overview==
+
<!--
-
Protein farnesyltransferase (FTase) catalyzes the transfer of the hydrophobic farnesyl group from farnesyl diphosphate (FPP) to cellular proteins such as Ras at a cysteine residue near their carboxy-terminus. This process is necessary for the subcellular localization of these proteins to the plasma membrane and is required for the transforming activity of oncogenic variants of Ras, making FTase a prime target for anticancer therapeutics. The high-resolution crystal structure of rat FTase was recently determined, and we present here the X-ray crystal structure of the first complex of FTase with a FPP substrate bound at the active site. The isoprenoid moiety of FPP binds in an extended conformation in a hydrophobic cavity of the beta subunit of the FTase enzyme, and the diphosphate moiety binds to a positively charged cleft at the top of this cavity near the subunit interface. The observed location of the FPP molecule is consistent with mutagenesis data. This binary complex of FTase with FPP leads us to suggest a "molecular ruler" hypothesis for isoprenoid substrate specificity, where the depth of the hydrophobic binding cavity acts as a ruler discriminating between isoprenoids of differing lengths. Although other length isoprenoids may bind in the cavity, only the 15-carbon farnesyl moiety binds with its C1 atom in register with a catalytic zinc ion as required for efficient transfer to the Ras substrate.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9657673}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9657673 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9657673}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Prenyltransferase]]
[[Category: Prenyltransferase]]
[[Category: Protein farnesyltransferase]]
[[Category: Protein farnesyltransferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:44:02 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:54:24 2008''

Revision as of 00:54, 1 July 2008

Image:1ft2.png

Template:STRUCTURE 1ft2

CO-CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A FARNESYL DIPHOSPHATE SUBSTRATE

Template:ABSTRACT PUBMED 9657673

About this Structure

1FT2 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate., Long SB, Casey PJ, Beese LS, Biochemistry. 1998 Jul 7;37(27):9612-8. PMID:9657673

Page seeded by OCA on Tue Jul 1 03:54:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ft2"
Personal tools