2i50

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2i50.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2i50.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2i50| PDB=2i50 | SCENE= }}
{{STRUCTURE_2i50| PDB=2i50 | SCENE= }}
-
'''Solution Structure of Ubp-M Znf-UBP domain'''
+
===Solution Structure of Ubp-M Znf-UBP domain===
-
==Overview==
+
<!--
-
The BUZ/Znf-UBP domain is a distinct ubiquitin-binding module found in the cytoplasmic deacetylase HDAC6, the E3 ubiquitin ligase BRAP2/IMP, and a subfamily of deubiquitinating enzymes. Here, we report the solution structure of the BUZ domain of Ubp-M, a ubiquitin-specific protease, and its interaction with ubiquitin. Unlike the BUZ domain from isopeptidase T (isoT) that contains a single zinc finger, the Ubp-M BUZ domain features three zinc-binding sites consisting of 12 residues. These zinc ligands form a pair of cross-braced ring fingers encapsulated within a third zinc finger in the primary structure. In contrast to isoT, which can form an N-terminal loop swapped dimer in the crystal state, the formation of additional zinc fingers in the Ubp-M BUZ domain restricts its N-terminal loop to intra-domain interactions. The ubiquitin-binding site of the Ubp-M BUZ domain is mapped to the highly conserved, concave surface formed by the alpha 3 helix and the central beta-sheet. We further show that this site binds to the C-terminal tail of free ubiquitin, and corresponding peptides display essentially the same binding affinities as full-length ubiquitin does for the Ubp-M BUZ domain. However, modification of the G76(Ub) carboxylate group either by a peptide or isopeptide bond abolishes BUZ-domain interaction. The unique ubiquitin-recognition mode of the BUZ domain family suggests that they may function as "sensors" of free ubiquitin in cells to achieve regulatory roles in many aspects of ubiquitin-dependent processes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17512543}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17512543 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17512543}}
==About this Structure==
==About this Structure==
-
2I50 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I50 OCA].
+
2I50 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I50 OCA].
==Reference==
==Reference==
Line 32: Line 36:
[[Category: Usp]]
[[Category: Usp]]
[[Category: Znf-ubp]]
[[Category: Znf-ubp]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:04:43 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:25:02 2008''

Revision as of 16:25, 27 July 2008

Image:2i50.png

Template:STRUCTURE 2i50

Solution Structure of Ubp-M Znf-UBP domain

Template:ABSTRACT PUBMED 17512543

About this Structure

2I50 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin., Pai MT, Tzeng SR, Kovacs JJ, Keaton MA, Li SS, Yao TP, Zhou P, J Mol Biol. 2007 Jul 6;370(2):290-302. Epub 2007 Apr 12. PMID:17512543

Page seeded by OCA on Sun Jul 27 19:25:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2i50"
Personal tools