1ags: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1ags.gif|left|200px]]
{{Seed}}
[[Image:1ags.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ags|  PDB=1ags  |  SCENE=  }}  
{{STRUCTURE_1ags|  PDB=1ags  |  SCENE=  }}  


'''A SURFACE MUTANT (G82R) OF A HUMAN ALPHA-GLUTATHIONE S-TRANSFERASE SHOWS DECREASED THERMAL STABILITY AND A NEW MODE OF MOLECULAR ASSOCIATION IN THE CRYSTAL'''
===A SURFACE MUTANT (G82R) OF A HUMAN ALPHA-GLUTATHIONE S-TRANSFERASE SHOWS DECREASED THERMAL STABILITY AND A NEW MODE OF MOLECULAR ASSOCIATION IN THE CRYSTAL===




==Overview==
<!--  
A chimeric enzyme (GST121) of the human alpha-glutathione S-transferases GST1-1 and GST2-2, which has improved catalytic efficiency and thermostability from its wild-type parent proteins, has been crystallized in a space group that is isomorphous with that reported for crystals of GST1-1. However, a single-site (G82R) mutant of GST121, which exhibits a significant reduction both in vitro and in vivo in protein thermostability, forms crystals that are not isomorphous with GST1-1. The mutant protein crystallizes in space group P2(1)2(1)2(1), with cell dimensions a = 49.5, b = 92.9, c = 115.9 A, and one dimer per asymmetric unit. Preliminary crystallographic results show that a mutation of the surface residue Gly 82 from a neutral to a charged residue causes new salt bridges to be formed among the GST dimers, suggesting that the G82R mutant might aggregate more readily than does GST121 in solution, resulting in a change of its solution properties.
The line below this paragraph, {{ABSTRACT_PUBMED_7892174}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7892174 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_7892174}}


==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Wang, B C.]]
[[Category: Wang, B C.]]
[[Category: Zeng, K.]]
[[Category: Zeng, K.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:15:01 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:49:08 2008''

Revision as of 13:49, 30 June 2008

File:1ags.png

Template:STRUCTURE 1ags

A SURFACE MUTANT (G82R) OF A HUMAN ALPHA-GLUTATHIONE S-TRANSFERASE SHOWS DECREASED THERMAL STABILITY AND A NEW MODE OF MOLECULAR ASSOCIATION IN THE CRYSTAL

Template:ABSTRACT PUBMED 7892174

About this Structure

1AGS is a Single protein structure of sequence from Synthetic construct. Full crystallographic information is available from OCA.

Reference

A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal., Zeng K, Rose JP, Chen HC, Strickland CL, Tu CP, Wang BC, Proteins. 1994 Nov;20(3):259-63. PMID:7892174

Page seeded by OCA on Mon Jun 30 16:49:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1ags&oldid=572621"