1uel
From Proteopedia
(New page: 200px<br /> <applet load="1uel" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uel" /> '''Solution structure of ubiquitin-like domain...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1uel.gif|left|200px]]<br /> | + | [[Image:1uel.gif|left|200px]]<br /><applet load="1uel" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1uel" size=" | + | |
caption="1uel" /> | caption="1uel" /> | ||
'''Solution structure of ubiquitin-like domain of hHR23B complexed with ubiquitin-interacting motif of proteasome subunit S5a'''<br /> | '''Solution structure of ubiquitin-like domain of hHR23B complexed with ubiquitin-interacting motif of proteasome subunit S5a'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ubiquitination, a modification in which single or multiple ubiquitin | + | Ubiquitination, a modification in which single or multiple ubiquitin molecules are attached to a protein, serves signaling functions that control several cellular processes. The ubiquitination signal is recognized by downstream effectors, many of which carry a ubiquitin-interacting motif (UIM). Such interactions can be modulated by regulators carrying a ubiquitin-like (UbL) domain, which binds UIM by mimicking ubiquitination. Of them, HR23B regulates the proteasomal targeting of ubiquitinated substrates, DNA repair factors, and other proteins. Here we report the structure of the UIM of the proteasome subunit S5a bound to the UbL domain of HR23B. The UbL domain presents one hydrophobic and two polar contact sites for interaction with UIM. The residues in these contact sites are well conserved in ubiquitin, but ubiquitin also presents a histidine at the interface. The pH-dependent protonation of this residue interferes with the access of ubiquitin to the UIM and the ubiquitin-associated domain (UBA), and its mutation to a smaller residue increases the affinity of ubiquitin for UIM. |
==About this Structure== | ==About this Structure== | ||
| - | 1UEL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1UEL is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1UEL OCA]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 16: | ||
[[Category: Hanaoka, H.]] | [[Category: Hanaoka, H.]] | ||
[[Category: Hiroaki, H.]] | [[Category: Hiroaki, H.]] | ||
| - | [[Category: Jee, J | + | [[Category: Jee, J G.]] |
[[Category: Kojima, C.]] | [[Category: Kojima, C.]] | ||
[[Category: Ohki, I.]] | [[Category: Ohki, I.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Shirakawa, M.]] | [[Category: Shirakawa, M.]] | ||
[[Category: Sugasawa, K.]] | [[Category: Sugasawa, K.]] | ||
| Line 31: | Line 30: | ||
[[Category: uim]] | [[Category: uim]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:37 2008'' |
Revision as of 13:23, 21 February 2008
|
Solution structure of ubiquitin-like domain of hHR23B complexed with ubiquitin-interacting motif of proteasome subunit S5a
Overview
Ubiquitination, a modification in which single or multiple ubiquitin molecules are attached to a protein, serves signaling functions that control several cellular processes. The ubiquitination signal is recognized by downstream effectors, many of which carry a ubiquitin-interacting motif (UIM). Such interactions can be modulated by regulators carrying a ubiquitin-like (UbL) domain, which binds UIM by mimicking ubiquitination. Of them, HR23B regulates the proteasomal targeting of ubiquitinated substrates, DNA repair factors, and other proteins. Here we report the structure of the UIM of the proteasome subunit S5a bound to the UbL domain of HR23B. The UbL domain presents one hydrophobic and two polar contact sites for interaction with UIM. The residues in these contact sites are well conserved in ubiquitin, but ubiquitin also presents a histidine at the interface. The pH-dependent protonation of this residue interferes with the access of ubiquitin to the UIM and the ubiquitin-associated domain (UBA), and its mutation to a smaller residue increases the affinity of ubiquitin for UIM.
About this Structure
1UEL is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the ubiquitin-interacting motif of S5a bound to the ubiquitin-like domain of HR23B., Fujiwara K, Tenno T, Sugasawa K, Jee JG, Ohki I, Kojima C, Tochio H, Hiroaki H, Hanaoka F, Shirakawa M, J Biol Chem. 2004 Feb 6;279(6):4760-7. Epub 2003 Oct 29. PMID:14585839
Page seeded by OCA on Thu Feb 21 15:23:37 2008
Categories: Homo sapiens | Protein complex | Fujiwara, K. | Hanaoka, H. | Hiroaki, H. | Jee, J G. | Kojima, C. | Ohki, I. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shirakawa, M. | Sugasawa, K. | Tenno, T. | Tochio, H. | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics | Ubl | Uim
