2ZJD
 
 | | Crystal Structure of LC3-p62 complex | | Descriptor: | Microtubule-associated proteins 1A/1B light chain 3B precursor, undecameric peptide from Sequestosome-1 | | Authors: | Ichimura, Y, Kumanomidou, T, Sou, Y, Mizushima, T, Ezaki, J, Ueno, T, Kominami, E, Yamane, T, Tanaka, K, Komatsu, M. | | Deposit date: | 2008-03-05 | | Release date: | 2008-06-03 | | Last modified: | 2023-11-01 | | Method: | X-RAY DIFFRACTION (1.56 Å) | | Cite: | Structural Basis for Sorting Mechanism of p62 in Selective Autophagy
J.Biol.Chem., 283, 2008
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3B0F
 | | Crystal structure of the UBA domain of p62 and its interaction with ubiquitin | | Descriptor: | SULFATE ION, Sequestosome-1 | | Authors: | Isogai, S, Morimoto, D, Arita, K, Unzai, S, Tenno, T, Hasegawa, J, Sou, Y, Komatsu, M, Tanaka, K, Shirakawa, M, Tochio, H. | | Deposit date: | 2011-06-09 | | Release date: | 2011-06-29 | | Last modified: | 2024-03-13 | | Method: | X-RAY DIFFRACTION (1.4 Å) | | Cite: | Crystal structure of the ubiquitin-associated (UBA) domain of p62 and its interaction with ubiquitin.
J.Biol.Chem., 286, 2011
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2D1I
 | | Structure of human Atg4b | | Descriptor: | Cysteine protease APG4B | | Authors: | Kumanomidou, T, Mizushima, T, Komatsu, M, Suzuki, A, Tanida, I, Sou, Y.S, Ueno, T, Kominami, E, Tanaka, K, Yamane, T. | | Deposit date: | 2005-08-24 | | Release date: | 2006-01-10 | | Last modified: | 2024-03-13 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | The Crystal Structure of Human Atg4b, a Processing and De-conjugating Enzyme for Autophagosome-forming Modifiers
J.Mol.Biol., 355, 2006
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2RRU
 | | Solution structure of the UBA omain of p62 and its interaction with ubiquitin | | Descriptor: | Sequestosome-1 | | Authors: | Isogai, S, Morimoto, D, Arita, K, Unzai, S, Tenno, T, Hasegawa, J, Sou, Y, Komatsu, M, Tanaka, K, Shirakawa, M, Tochio, H. | | Deposit date: | 2011-06-09 | | Release date: | 2011-06-29 | | Last modified: | 2023-06-14 | | Method: | SOLUTION NMR | | Cite: | Crystal structure of the UBA omain of p62 and its interaction with ubiquitin
To be Published
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