4dbg: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:4dbg.jpg|left|200px]] | |||
The | <!-- | ||
The line below this paragraph, containing "STRUCTURE_4dbg", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_4dbg| PDB=4dbg | SCENE= }} | |||
===Crystal structure of HOIL-1L-UBL complexed with HOIP-UBA derivative=== | |||
<!-- | |||
The line below this paragraph, {{ABSTRACT_PUBMED_22430200}}, adds the Publication Abstract to the page | |||
(as it appears on PubMed at http://www.pubmed.gov), where 22430200 is the PubMed ID number. | |||
--> | |||
{{ABSTRACT_PUBMED_22430200}} | |||
==About this Structure== | |||
[[4dbg]] is a 2 chain structure with 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=4DBG OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:022430200</ref><references group="xtra"/> | |||
[[Category: Homo sapiens]] | |||
[[Category: Hiromoto, T.]] | |||
[[Category: Kato, K.]] | |||
[[Category: Kurimoto, E.]] | |||
[[Category: Mizushima, T.]] | |||
[[Category: Yagi, H.]] | |||
[[Category: Ligase]] | |||
[[Category: Ubiquitin fold]] | |||
[[Category: Ubiquitination]] | |||
Revision as of 06:06, 4 April 2012
Crystal structure of HOIL-1L-UBL complexed with HOIP-UBA derivative
Template:ABSTRACT PUBMED 22430200
About this Structure
4dbg is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Yagi H, Ishimoto K, Hiromoto T, Fujita H, Mizushima T, Uekusa Y, Yagi-Utsumi M, Kurimoto E, Noda M, Uchiyama S, Tokunaga F, Iwai K, Kato K. A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex. EMBO Rep. 2012 Mar 20. doi: 10.1038/embor.2012.24. PMID:22430200 doi:10.1038/embor.2012.24
