1ify
From Proteopedia
(New page: 200px<br /> <applet load="1ify" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ify" /> '''Solution Structure of the Internal UBA Doma...) |
|||
| Line 20: | Line 20: | ||
[[Category: ubiquitin proteosome pathway]] | [[Category: ubiquitin proteosome pathway]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:29:25 2007'' |
Revision as of 15:22, 12 November 2007
|
Solution Structure of the Internal UBA Domain of HHR23A
Overview
UBA domains are a commonly occurring sequence motif of approximately 45, amino acid residues that are found in diverse proteins involved in the, ubiquitin/proteasome pathway, DNA excision-repair, and cell signaling via, protein kinases. The human homologue of yeast Rad23A (HHR23A) is one, example of a nucleotide excision-repair protein that contains both an, internal and a C-terminal UBA domain. The solution structure of HHR23A, UBA(2) showed that the domain forms a compact three-helix bundle. We, report the structure of the internal UBA(1) domain of HHR23A. Comparison, of the structures of UBA(1) and UBA(2) reveals that both form very similar, folds and have a conserved large hydrophobic surface patch. The structural, similarity between UBA(1) and UBA(2), in spite of their low level of, sequence conservation, leads us to conclude that the structural, variability of UBA domains in general is likely to be rather small. On the, basis of the structural similarities as well as analysis of sequence, conservation, we predict that this hydrophobic surface patch is a common, protein-interacting surface present in diverse UBA domains. Furthermore, accumulating evidence that ubiquitin binds to UBA domains leads us to the, prediction that the hydrophobic surface patch of UBA domains interacts, with the hydrophobic surface on the five-stranded beta-sheet of ubiquitin., Detailed comparison of the structures of the two UBA domains, combined, with previous mutagenesis studies, indicates that the binding site of, HIV-1 Vpr on UBA(2) does not completely overlap the ubiquitin binding, site.
About this Structure
1IFY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions., Mueller TD, Feigon J, J Mol Biol. 2002 Jun 21;319(5):1243-55. PMID:12079361
Page seeded by OCA on Mon Nov 12 17:29:25 2007
