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.


2je4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2je4.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2je4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2je4| PDB=2je4 | SCENE= }}
{{STRUCTURE_2je4| PDB=2je4 | SCENE= }}
-
'''ATOMIC-RESOLUTION CRYSTAL STRUCTURE OF CHEMICALLY-SYNTHESIZED HIV-1 PROTEASE IN COMPLEX WITH JG-365'''
+
===ATOMIC-RESOLUTION CRYSTAL STRUCTURE OF CHEMICALLY-SYNTHESIZED HIV-1 PROTEASE IN COMPLEX WITH JG-365===
-
==Overview==
+
<!--
-
As part of our ongoing studies of the human immunodeficiency virus type 1 (HIV-1) protease enzyme, we set out to develop a modular chemical synthesis of the protein from multiple peptide segments. Our initial attempts were frustrated by the insolubility of intermediate peptide products. To overcome this problem, we designed a synthetic strategy combining the solubility-enhancing properties of C-terminal (Arg)n tags and the biological phenomenon of autoprocessing of the Gag-Pol polyprotein that occurs during maturation of the HIV-1 virus in vivo. Synthesis of a 119-residue peptide chain containing 10 residues of the reverse transcriptase (RT) open reading frame plus an (Arg)(10) tag at the C-terminus was straightforward by native chemical ligation followed by conversion of the Cys residues to Ala by Raney nickel desulfurization. The product polypeptide itself completed the final synthetic step by removing the C-terminal modification under folding conditions, to give the mature 99-residue polypeptide. High-purity homodimeric HIV-1 protease protein was obtained in excellent yield and had full enzymatic activity; the structure of the synthetic enzyme was confirmed by X-ray crystallography to a resolution of 1.07 A. This efficient modular synthesis by a biomimetic autoprocessing strategy will enable the facile synthesis of unique chemical analogues of the HIV-1 protease to further elucidate the molecular basis of enzyme catalysis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17705484}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17705484 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17705484}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Protease]]
[[Category: Protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:45:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 10 12:37:02 2008''

Revision as of 09:37, 10 July 2008

Image:2je4.png

Template:STRUCTURE 2je4

ATOMIC-RESOLUTION CRYSTAL STRUCTURE OF CHEMICALLY-SYNTHESIZED HIV-1 PROTEASE IN COMPLEX WITH JG-365

Template:ABSTRACT PUBMED 17705484

About this Structure

2JE4 is a Protein complex structure of sequences from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

Modular total chemical synthesis of a human immunodeficiency virus type 1 protease., Johnson EC, Malito E, Shen Y, Rich D, Tang WJ, Kent SB, J Am Chem Soc. 2007 Sep 19;129(37):11480-90. Epub 2007 Aug 18. PMID:17705484

Page seeded by OCA on Thu Jul 10 12:37:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2je4"
Personal tools