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.


1iyk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1iyk.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1iyk.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1iyk| PDB=1iyk | SCENE= }}
{{STRUCTURE_1iyk| PDB=1iyk | SCENE= }}
-
'''CRYSTAL STRUCTURE OF CANDIDA ALBICANS N-MYRISTOYLTRANSFERASE WITH MYRISTOYL-COA AND PEPTIDIC INHIBITOR'''
+
===CRYSTAL STRUCTURE OF CANDIDA ALBICANS N-MYRISTOYLTRANSFERASE WITH MYRISTOYL-COA AND PEPTIDIC INHIBITOR===
-
==Overview==
+
<!--
-
Myristoyl-CoA:protein N-myristoyltransferase (Nmt) is a monomeric enzyme that catalyzes the transfer of the fatty acid myristate from myristoyl-CoA to the N-terminal glycine residue of a variety of eukaryotic and viral proteins. Genetic and biochemical studies have established that Nmt is an attractive target for antifungal drugs. We present here crystal structures of C. albicans Nmt complexed with two classes of inhibitor competitive for peptide substrates. One is a peptidic inhibitor designed from the peptide substrate; the other is a nonpeptidic inhibitor having a benzofuran core. Both inhibitors are bound into the same binding groove, generated by some structural rearrangements of the enzyme, with the peptidic inhibitor showing a substrate-like binding mode and the nonpeptidic inhibitor binding differently. Further, site-directed mutagenesis for C. albicans Nmt has been utilized in order to define explicitly which amino acids are critical for inhibitor binding. The results suggest that the enzyme has some degree of flexibility for substrate binding and provide valuable information for inhibitor design.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12401496}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12401496 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12401496}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Winkler, F K.]]
[[Category: Winkler, F K.]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:35:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:13:45 2008''

Revision as of 11:13, 1 July 2008

Image:1iyk.png

Template:STRUCTURE 1iyk

CRYSTAL STRUCTURE OF CANDIDA ALBICANS N-MYRISTOYLTRANSFERASE WITH MYRISTOYL-COA AND PEPTIDIC INHIBITOR

Template:ABSTRACT PUBMED 12401496

About this Structure

1IYK is a Single protein structure of sequence from Candida albicans. Full crystallographic information is available from OCA.

Reference

Crystal structures of Candida albicans N-myristoyltransferase with two distinct inhibitors., Sogabe S, Masubuchi M, Sakata K, Fukami TA, Morikami K, Shiratori Y, Ebiike H, Kawasaki K, Aoki Y, Shimma N, D'Arcy A, Winkler FK, Banner DW, Ohtsuka T, Chem Biol. 2002 Oct;9(10):1119-28. PMID:12401496

Page seeded by OCA on Tue Jul 1 14:13:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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