1s1q
From Proteopedia
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| - | [[Image:1s1q.gif|left|200px]] | + | [[Image:1s1q.gif|left|200px]] |
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| - | '''TSG101(UEV) domain in complex with Ubiquitin''' | + | {{Structure |
| + | |PDB= 1s1q |SIZE=350|CAPTION= <scene name='initialview01'>1s1q</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''TSG101(UEV) domain in complex with Ubiquitin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1S1Q is a [ | + | 1S1Q is a [[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=1S1Q OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15053872 15053872] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: heterodimer]] | [[Category: heterodimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:59:14 2008'' |
Revision as of 11:59, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 20 13:59:14 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
