1f4i: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 1: Line 1:
[[Image:1f4i.jpg|left|200px]]
{{Seed}}
[[Image:1f4i.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1f4i|  PDB=1f4i  |  SCENE=  }}  
{{STRUCTURE_1f4i|  PDB=1f4i  |  SCENE=  }}  


'''SOLUTION STRUCTURE OF THE HHR23A UBA(2) MUTANT P333E, DEFICIENT IN BINDING THE HIV-1 ACCESSORY PROTEIN VPR'''
===SOLUTION STRUCTURE OF THE HHR23A UBA(2) MUTANT P333E, DEFICIENT IN BINDING THE HIV-1 ACCESSORY PROTEIN VPR===




==Overview==
<!--
The DNA repair protein HHR23A is a highly conserved protein that functions in nucleotide excision repair. HHR23A contains two ubiquitin associated domains (UBA) that are conserved in a number of proteins with diverse functions involved in ubiquitination, UV excision repair, and signaling pathways via protein kinases. The cellular binding partners of UBA domains remain unclear; however, we previously found that the HHR23A UBA(2) domain interacts specifically with the HIV-1 Vpr protein. Analysis of the low resolution solution structure of HHR23A UBA(2) revealed a hydrophobic loop region of the UBA(2) domain that we predicted was the interface for protein/protein interactions. Here we present results of in vitro binding studies that demonstrate the requirement of this hydrophobic loop region for interaction with human immunodeficiency virus (HIV-1) Vpr. A single point mutation of the Pro at residue 333 to a Glu totally abolishes the binding of HIV-1 Vpr to UBA(2). High resolution NMR structures of the binding deficient UBA(2) mutant P333E as well as of the wild-type UBA(2) domain were determined to compare the effect of this mutation on the structure. Small but significant differences are observed only locally at the site of the mutation. The biochemical and structural analysis confirms the function of the HHR23A UBA(2) GFP-loop as the protein/protein interacting domain.
The line below this paragraph, {{ABSTRACT_PUBMED_11087358}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11087358 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11087358}}


==About this Structure==
==About this Structure==
1F4I is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4I OCA].  
1F4I is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4I OCA].  


==Reference==
==Reference==
Line 26: Line 30:
[[Category: Withers-Ward, E S.]]
[[Category: Withers-Ward, E S.]]
[[Category: Alpha helical bundle]]
[[Category: Alpha helical bundle]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:53:18 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:40:33 2008''

Revision as of 23:40, 30 June 2008

File:1f4i.png

Template:STRUCTURE 1f4i

SOLUTION STRUCTURE OF THE HHR23A UBA(2) MUTANT P333E, DEFICIENT IN BINDING THE HIV-1 ACCESSORY PROTEIN VPR

Template:ABSTRACT PUBMED 11087358

About this Structure

1F4I is a Single protein structure. Full experimental information is available from OCA.

Reference

Biochemical and structural analysis of the interaction between the UBA(2) domain of the DNA repair protein HHR23A and HIV-1 Vpr., Withers-Ward ES, Mueller TD, Chen IS, Feigon J, Biochemistry. 2000 Nov 21;39(46):14103-12. PMID:11087358

Page seeded by OCA on Tue Jul 1 02:40:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1f4i&oldid=595507"