From Proteopedia
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| - | [[Image:2al3.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2al3| PDB=2al3 | SCENE= }} | | {{STRUCTURE_2al3| PDB=2al3 | SCENE= }} |
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| - | '''Solution structure and backbone dynamics of an N-terminal ubiquitin-like domain in the GLUT4-tethering protein, TUG'''
| + | ===Solution structure and backbone dynamics of an N-terminal ubiquitin-like domain in the GLUT4-tethering protein, TUG=== |
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| - | ==Overview==
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| - | The GLUT4-regulating protein, TUG, functions to retain GLUT4-containing membrane vesicles intracellularly and, in response to insulin stimulation, releases these vesicles to the cellular exocytic machinery for translocation to the plasma membrane. As part of our on going effort to describe the molecular basis for TUG function, we have determined the tertiary structure and characterized the backbone dynamics for an N-terminal ubiquitin-like domain (TUG-UBL1) using NMR spectroscopy. A well-ordered conformation is observed for residues 10-83 of full-length TUG, and confirms a beta-grasp or ubiquitin-like topology. Although not required for in vitro association with GLUT4, the functional role of the TUG-UBL1 domain has not yet been described. We undertook a limited literature review of similar N-terminal UBL domains and noted that a majority participate in protein-protein interactions, generally functioning as adaptor modules to physically associate the over all activity of the protein with a specific cellular process, such as the ubiquitin-proteasome pathway. In consistent fashion, TUG-UBL1 is not expected to participate in a covalent protein modification reaction as it lacks the characteristic C-terminal diglycine ("GG") motif required for conjugation to an acceptor lysine, and also lacks the three most common acceptor lysine residues involved in polyubiquitination. Additionally, analysis of the TUG-UBL1 molecular surface reveals a lack of conservation of the "Ile-44 hydrophobic face" typically involved in ubiquitin recognition. Instead, we speculate on the possible significance of a concentrated area of negative electrostatic potential with increased backbone mobility, both of which are features suggestive of a potential protein-protein interaction site. | + | The line below this paragraph, {{ABSTRACT_PUBMED_16501224}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16501224 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16501224}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 2AL3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AL3 OCA]. | + | 2AL3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AL3 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Yu, C.]] | | [[Category: Yu, C.]] |
| | [[Category: Tug ubl1 insulin]] | | [[Category: Tug ubl1 insulin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:10:46 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:18:31 2008'' |
Revision as of 11:18, 29 July 2008
Template:STRUCTURE 2al3
Solution structure and backbone dynamics of an N-terminal ubiquitin-like domain in the GLUT4-tethering protein, TUG
Template:ABSTRACT PUBMED 16501224
About this Structure
2AL3 is a Single protein structure of sequence from Mus musculus. Full experimental information is available from OCA.
Reference
Solution structure and backbone dynamics of an N-terminal ubiquitin-like domain in the GLUT4-regulating protein, TUG., Tettamanzi MC, Yu C, Bogan JS, Hodsdon ME, Protein Sci. 2006 Mar;15(3):498-508. PMID:16501224
Page seeded by OCA on Tue Jul 29 14:18:31 2008
