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.

1ied

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ied.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ied.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ied| PDB=1ied | SCENE= }}
{{STRUCTURE_1ied| PDB=1ied | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157E) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE'''
+
===CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157E) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE===
-
==Overview==
+
<!--
-
Herpesvirus proteases belong to a new class of serine proteases and contain a novel Ser-His-His catalytic triad, while classical serine proteases have an acidic residue as the third member. To gain a better understanding of the molecular basis for the functional role of the third-member His residue, we have carried out structural and biochemical investigations of human cytomegalovirus (HCMV) protease that bears mutations of the His157 third member. Kinetic studies showed that all the mutants have reduced catalytic activity. Structural studies revealed that a solvent molecule is hydrogen-bonded to the His63 second member and Ser134 in the H157A mutant, partly rescuing the activity of this mutant. This is confirmed by our kinetic and structural observations on the S134A/H157A double mutant, which showed further reductions in the catalytic activity. The structure of the H157A mutant is also in complex with the PMSF inhibitor. The H157E mutant has the best catalytic activity among the mutants; its structure, however, showed conformational readjustments of the His63 and Ser132 residues. The Ser132-His63 diad of HCMV protease has similar activity as the diads in classical serine proteases, whereas the contribution of the His157 third member to the catalysis is much smaller. Finally, structural comparisons revealed the presence of two conserved structural water molecules at the bottom of the S(1) pocket, suggesting a possible new direction for the design of HCMV protease inhibitors.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11371196}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11371196 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11371196}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Viral protease]]
[[Category: Viral protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:54:30 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:50:24 2008''

Revision as of 07:50, 1 July 2008

Image:1ied.png

Template:STRUCTURE 1ied

CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157E) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE

Template:ABSTRACT PUBMED 11371196

About this Structure

1IED is a Single protein structure of sequence from Human herpesvirus 5. Full crystallographic information is available from OCA.

Reference

Investigating the role of histidine 157 in the catalytic activity of human cytomegalovirus protease., Khayat R, Batra R, Massariol MJ, Lagace L, Tong L, Biochemistry. 2001 May 29;40(21):6344-51. PMID:11371196

Page seeded by OCA on Tue Jul 1 10:50:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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