This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2hth
From Proteopedia
(New page: 200px<br /> <applet load="2hth" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hth, resolution 2.70Å" /> '''Structural basis fo...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2hth. | + | [[Image:2hth.jpg|left|200px]]<br /><applet load="2hth" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2hth" size=" | + | |
caption="2hth, resolution 2.70Å" /> | caption="2hth, resolution 2.70Å" /> | ||
'''Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domain'''<br /> | '''Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domain'''<br /> | ||
| Line 6: | Line 5: | ||
==Overview== | ==Overview== | ||
The ESCRT-I and ESCRT-II complexes help sort ubiquitinated proteins into, vesicles that accumulate within multivesicular bodies (MVBs)., Crystallographic and biochemical analyses reveal that the GLUE domain of, the human ESCRT-II EAP45 (also called VPS36) subunit is a split, pleckstrin-homology domain that binds ubiquitin along one edge of the, beta-sandwich. The structure suggests how human ESCRT-II can couple, recognition of ubiquitinated cargoes and endosomal phospholipids during, MVB protein sorting. | The ESCRT-I and ESCRT-II complexes help sort ubiquitinated proteins into, vesicles that accumulate within multivesicular bodies (MVBs)., Crystallographic and biochemical analyses reveal that the GLUE domain of, the human ESCRT-II EAP45 (also called VPS36) subunit is a split, pleckstrin-homology domain that binds ubiquitin along one edge of the, beta-sandwich. The structure suggests how human ESCRT-II can couple, recognition of ubiquitinated cargoes and endosomal phospholipids during, MVB protein sorting. | ||
| + | |||
| + | ==Disease== | ||
| + | Known disease associated with this structure: Cleft palate, isolated OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191339 191339]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2HTH 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:// | + | 2HTH 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=2HTH OCA]. |
==Reference== | ==Reference== | ||
| Line 24: | Line 26: | ||
[[Category: viral budding]] | [[Category: viral budding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:33:36 2008'' |
Revision as of 15:33, 15 February 2008
|
Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domain
Contents |
Overview
The ESCRT-I and ESCRT-II complexes help sort ubiquitinated proteins into, vesicles that accumulate within multivesicular bodies (MVBs)., Crystallographic and biochemical analyses reveal that the GLUE domain of, the human ESCRT-II EAP45 (also called VPS36) subunit is a split, pleckstrin-homology domain that binds ubiquitin along one edge of the, beta-sandwich. The structure suggests how human ESCRT-II can couple, recognition of ubiquitinated cargoes and endosomal phospholipids during, MVB protein sorting.
Disease
Known disease associated with this structure: Cleft palate, isolated OMIM:[191339]
About this Structure
2HTH is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for ubiquitin recognition by the human ESCRT-II EAP45 GLUE domain., Alam SL, Langelier C, Whitby FG, Koirala S, Robinson H, Hill CP, Sundquist WI, Nat Struct Mol Biol. 2006 Nov;13(11):1029-30. Epub 2006 Oct 22. PMID:17057716
Page seeded by OCA on Fri Feb 15 17:33:36 2008
