1s1q
From Proteopedia
(New page: 200px<br /> <applet load="1s1q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s1q, resolution 2.00Å" /> '''TSG101(UEV) domain ...) |
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| - | [[Image:1s1q.gif|left|200px]]<br /> | + | [[Image:1s1q.gif|left|200px]]<br /><applet load="1s1q" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1s1q, resolution 2.00Å" /> | caption="1s1q, resolution 2.00Å" /> | ||
'''TSG101(UEV) domain in complex with Ubiquitin'''<br /> | '''TSG101(UEV) domain in complex with Ubiquitin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The UEV domain of the TSG101 protein functions in both HIV-1 budding and | + | The UEV domain of the TSG101 protein functions in both HIV-1 budding and the vacuolar protein sorting (VPS) pathway, where it binds ubiquitylated proteins as they are sorted into vesicles that bud into late endosomal compartments called multivesicular bodies (MVBs). TSG101 UEV-ubiquitin interactions are therefore important for delivery of both substrates and hydrolytic enzymes to lysosomes, which receive proteins via fusion with MVBs. Here, we report the crystal structure of the TSG101 UEV domain in complex with ubiquitin at 2.0 A resolution. TSG101 UEV contacts the Ile44 surface and an adjacent loop of ubiquitin through a highly solvated interface. Mutations that disrupt the interface inhibit MVB sorting, and the structure also explains how the TSG101 UEV can independently bind its ubiquitin and Pro-Thr/Ser-Ala-Pro peptide ligands. Remarkably, comparison with mapping data from other UEV and related E2 proteins indicates that although the different E2/UEV domains share the same structure and have conserved ubiquitin binding activity, they bind through very different interfaces. |
==Disease== | ==Disease== | ||
| - | Known | + | Known diseases associated with this structure: Breast cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601387 601387]], Cleft palate, isolated OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191339 191339]] |
==About this Structure== | ==About this Structure== | ||
| - | 1S1Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CU, SO4 and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1S1Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S1Q OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Hill, C | + | [[Category: Hill, C P.]] |
| - | [[Category: Hill, G | + | [[Category: Hill, G C.]] |
| - | [[Category: Holton, J | + | [[Category: Holton, J M.]] |
| - | [[Category: Kelly, B | + | [[Category: Kelly, B N.]] |
| - | [[Category: Schubert, H | + | [[Category: Schubert, H L.]] |
| - | [[Category: Sundquist, W | + | [[Category: Sundquist, W I.]] |
[[Category: ACY]] | [[Category: ACY]] | ||
[[Category: CU]] | [[Category: CU]] | ||
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[[Category: heterodimer]] | [[Category: heterodimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:57:03 2008'' |
Revision as of 12:57, 21 February 2008
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TSG101(UEV) domain in complex with Ubiquitin
Contents |
Overview
The UEV domain of the TSG101 protein functions in both HIV-1 budding and the vacuolar protein sorting (VPS) pathway, where it binds ubiquitylated proteins as they are sorted into vesicles that bud into late endosomal compartments called multivesicular bodies (MVBs). TSG101 UEV-ubiquitin interactions are therefore important for delivery of both substrates and hydrolytic enzymes to lysosomes, which receive proteins via fusion with MVBs. Here, we report the crystal structure of the TSG101 UEV domain in complex with ubiquitin at 2.0 A resolution. TSG101 UEV contacts the Ile44 surface and an adjacent loop of ubiquitin through a highly solvated interface. Mutations that disrupt the interface inhibit MVB sorting, and the structure also explains how the TSG101 UEV can independently bind its ubiquitin and Pro-Thr/Ser-Ala-Pro peptide ligands. Remarkably, comparison with mapping data from other UEV and related E2 proteins indicates that although the different E2/UEV domains share the same structure and have conserved ubiquitin binding activity, they bind through very different interfaces.
Disease
Known diseases associated with this structure: Breast cancer OMIM:[601387], Cleft palate, isolated OMIM:[191339]
About this Structure
1S1Q is a Protein complex structure of sequences from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
Ubiquitin recognition by the human TSG101 protein., Sundquist WI, Schubert HL, Kelly BN, Hill GC, Holton JM, Hill CP, Mol Cell. 2004 Mar 26;13(6):783-9. PMID:15053872
Page seeded by OCA on Thu Feb 21 14:57:03 2008
Categories: Homo sapiens | Protein complex | Hill, C P. | Hill, G C. | Holton, J M. | Kelly, B N. | Schubert, H L. | Sundquist, W I. | ACY | CU | SO4 | Heterodimer
