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.


1bl3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 5: Line 5:
==Overview==
==Overview==
-
Human immunodeficiency virus (HIV) integrase is the enzyme responsible for, insertion of a DNA copy of the viral genome into host DNA, an essential, step in the replication cycle of HIV. HIV-1 integrase comprises three, functional and structural domains: an N-terminal zinc-binding domain, a, catalytic core domain and a C-terminal DNA-binding domain. The catalytic, core domain with the F185H mutation has been crystallized without sodium, cacodylate in a new crystal form, free and complexed with the catalytic, metal Mg2+. The structures have been determined and refined to about 2.2, A. Unlike the previously reported structures, the three active-site, carboxylate residues (D,D-35-E motif) are well ordered and both aspartate, residues delineate a proper metal-binding site. Comparison of the ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9735293 (full description)]]
+
Human immunodeficiency virus (HIV) integrase is the enzyme responsible for, insertion of a DNA copy of the viral genome into host DNA, an essential, step in the replication cycle of HIV. HIV-1 integrase comprises three, functional and structural domains: an N-terminal zinc-binding domain, a, catalytic core domain and a C-terminal DNA-binding domain. The catalytic, core domain with the F185H mutation has been crystallized without sodium, cacodylate in a new crystal form, free and complexed with the catalytic, metal Mg2+. The structures have been determined and refined to about 2.2, A. Unlike the previously reported structures, the three active-site, carboxylate residues (D,D-35-E motif) are well ordered and both aspartate, residues delineate a proper metal-binding site. Comparison of the active, binding site of this domain with that of other members from the, polynucleotidyl transferases superfamily shows a high level of similarity, providing a confident template for the design of antiviral agents.
==About this Structure==
==About this Structure==
-
1BL3 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]] with MG as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BL3 OCA]].
+
1BL3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: ACT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BL3 OCA].
==Reference==
==Reference==
Line 28: Line 28:
[[Category: polyprotein]]
[[Category: polyprotein]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:55:43 2007''
+
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:02:09 2007''

Revision as of 12:56, 5 November 2007


1bl3, resolution 2.00Å

Drag the structure with the mouse to rotate

CATALYTIC DOMAIN OF HIV-1 INTEGRASE

Overview

Human immunodeficiency virus (HIV) integrase is the enzyme responsible for, insertion of a DNA copy of the viral genome into host DNA, an essential, step in the replication cycle of HIV. HIV-1 integrase comprises three, functional and structural domains: an N-terminal zinc-binding domain, a, catalytic core domain and a C-terminal DNA-binding domain. The catalytic, core domain with the F185H mutation has been crystallized without sodium, cacodylate in a new crystal form, free and complexed with the catalytic, metal Mg2+. The structures have been determined and refined to about 2.2, A. Unlike the previously reported structures, the three active-site, carboxylate residues (D,D-35-E motif) are well ordered and both aspartate, residues delineate a proper metal-binding site. Comparison of the active, binding site of this domain with that of other members from the, polynucleotidyl transferases superfamily shows a high level of similarity, providing a confident template for the design of antiviral agents.

About this Structure

1BL3 is a Single protein structure of sequence from Human immunodeficiency virus 1 with MG as ligand. Structure known Active Site: ACT. Full crystallographic information is available from OCA.

Reference

Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: high level of similarity of the active site with other viral integrases., Maignan S, Guilloteau JP, Zhou-Liu Q, Clement-Mella C, Mikol V, J Mol Biol. 1998 Sep 18;282(2):359-68. PMID:9735293

Page seeded by OCA on Mon Nov 5 15:02:09 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools