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.

3phv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3phv.gif|left|200px]]
+
{{Seed}}
 +
[[Image:3phv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3phv| PDB=3phv | SCENE= }}
{{STRUCTURE_3phv| PDB=3phv | SCENE= }}
-
'''X-RAY ANALYSIS OF HIV-1 PROTEINASE AT 2.7 ANGSTROMS RESOLUTION CONFIRMS STRUCTURAL HOMOLOGY AMONG RETROVIRAL ENZYMES'''
+
===X-RAY ANALYSIS OF HIV-1 PROTEINASE AT 2.7 ANGSTROMS RESOLUTION CONFIRMS STRUCTURAL HOMOLOGY AMONG RETROVIRAL ENZYMES===
-
==Overview==
+
<!--
-
Knowledge of the tertiary structure of the proteinase from human immunodeficiency virus HIV-1 is important to the design of inhibitors that might possess antiviral activity and thus be useful in the treatment of AIDS. The conserved Asp-Thr/Ser-Gly sequence in retroviral proteinases suggests that they exist as dimers similar to the ancestor proposed for the pepsins. Although this has been confirmed by X-ray analyses of Rous sarcoma virus and HIV-1 proteinases, these structures have overall folds that are similar to each other only where they are also similar to the pepsins. We now report a further X-ray analysis of a recombinant HIV-1 proteinase at 2.7 A resolution. The polypeptide chain adopts a fold in which the N- and C-terminal strands are organized together in a four-stranded beta-sheet. A helix precedes the single C-terminal strand, as in the Rous sarcoma virus proteinase and also in a synthetic HIV-1 proteinase, in which the cysteines have been replaced by alpha-aminobuytric acid. The structure reported here provides an explanation for the amino acid invariance amongst retroviral proteinases, but differs from that reported earlier in some residues that are candidates for substrate interactions at P3, and in the mode of intramolecular cleavage during processing of the polyprotein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_2682266}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 2682266 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_2682266}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Wilderspin, A.]]
[[Category: Wilderspin, A.]]
[[Category: Wood, S P.]]
[[Category: Wood, S P.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:10:36 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:02:17 2008''

Revision as of 10:02, 3 July 2008

Image:3phv.png

Template:STRUCTURE 3phv

X-RAY ANALYSIS OF HIV-1 PROTEINASE AT 2.7 ANGSTROMS RESOLUTION CONFIRMS STRUCTURAL HOMOLOGY AMONG RETROVIRAL ENZYMES

Template:ABSTRACT PUBMED 2682266

About this Structure

3PHV is a Single protein structure of sequence from Human immunodeficiency virus type 1 (isolate hxb2). Full crystallographic information is available from OCA.

Reference

X-ray analysis of HIV-1 proteinase at 2.7 A resolution confirms structural homology among retroviral enzymes., Lapatto R, Blundell T, Hemmings A, Overington J, Wilderspin A, Wood S, Merson JR, Whittle PJ, Danley DE, Geoghegan KF, et al., Nature. 1989 Nov 16;342(6247):299-302. PMID:2682266

Page seeded by OCA on Thu Jul 3 13:02:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3phv"
Personal tools