<p>Ub is colored in mauve taupe. <b>A</b>) Cartoon representation of Ub. Residues mediating interaction with NOD1 CARD are shown as sticks and are colored red. The canonical hydrophobic pocket residues are shown as sticks and colored black. <b>B</b>) Surface views of the NOD1 CARD interaction site on Ub. <b>C</b>) Surface views of the Phe4 hydrophobic patch (F4 patch) on Ub alone (green) and merged with the NOD1 CARD site (yellow). <b>D</b>) Surface views of one site on Ub recognized by the NZF domain of HOIL-1L alone (green) and merged with the NOD1 CARD site (yellow). This domain specifically recognizes linear chains of Ub by binding to the hydrophobic pocket of the distal Ub and to an area surrounding Phe4 of the proximal Ub of a linear ...
The structurally defined ubiquitin-like homology fold (UBL) can engage in several unique protein-pro...
Conserved hydrophobic core residues are indicated by *, and totally conserved residues by #. The blu...
<p><b>A</b>) Ribbon representation of an alignment of K48-linked diubiquitin structures. The proxima...
<p><b>A</b>) The NOD1 CARD dimer from our crystal structure (CARD A, cyan and CARD B, blue) is depic...
<p>The sidechains of Phe4 (purple) and Ile44 (black) from Ub and Cys59 (red) and Tyr88 (green) are s...
<p><b>A,</b> Domain architecture of USP5. NT, N-terminal domain; ZnF, zinc-finger domain; UBA1 and U...
<p><b>A</b>) NOD1 CARD and Ub crystallized as a dimer of dimers. NOD1 CARD A (cyan) and Ub C (mauve ...
<p><b>A,</b> DC-UbP contains two separate domains, the N-terminal UBD and the C-terminal UbL. The N-...
DC-UbP/UBTD2 is a ubiquitin (Ub) domain-containing protein first identified from dendritic cells, an...
<p>The ubiquitin hydrophobic patch residues are shown in magenta. PLpro residues identified through ...
Abstract Poly-ubiquitin (poly-Ub) is involved in various cellular processes through the linkage-spec...
Ubiquitin is a small protein that is covalently attached to proteins, either as a single ubiquitin m...
<p>(A) A grey bar, representing the domain organization of the UbxIb transcription factor shows the ...
The Caspase Recruitment Domain (CARD) from the innate immune receptor NOD1 was crystallized with Ubi...
<p>(A) Mapping of intramolecular crosslinking sites on the Utp21 tandem WD domain structure. Crossli...
The structurally defined ubiquitin-like homology fold (UBL) can engage in several unique protein-pro...
Conserved hydrophobic core residues are indicated by *, and totally conserved residues by #. The blu...
<p><b>A</b>) Ribbon representation of an alignment of K48-linked diubiquitin structures. The proxima...
<p><b>A</b>) The NOD1 CARD dimer from our crystal structure (CARD A, cyan and CARD B, blue) is depic...
<p>The sidechains of Phe4 (purple) and Ile44 (black) from Ub and Cys59 (red) and Tyr88 (green) are s...
<p><b>A,</b> Domain architecture of USP5. NT, N-terminal domain; ZnF, zinc-finger domain; UBA1 and U...
<p><b>A</b>) NOD1 CARD and Ub crystallized as a dimer of dimers. NOD1 CARD A (cyan) and Ub C (mauve ...
<p><b>A,</b> DC-UbP contains two separate domains, the N-terminal UBD and the C-terminal UbL. The N-...
DC-UbP/UBTD2 is a ubiquitin (Ub) domain-containing protein first identified from dendritic cells, an...
<p>The ubiquitin hydrophobic patch residues are shown in magenta. PLpro residues identified through ...
Abstract Poly-ubiquitin (poly-Ub) is involved in various cellular processes through the linkage-spec...
Ubiquitin is a small protein that is covalently attached to proteins, either as a single ubiquitin m...
<p>(A) A grey bar, representing the domain organization of the UbxIb transcription factor shows the ...
The Caspase Recruitment Domain (CARD) from the innate immune receptor NOD1 was crystallized with Ubi...
<p>(A) Mapping of intramolecular crosslinking sites on the Utp21 tandem WD domain structure. Crossli...
The structurally defined ubiquitin-like homology fold (UBL) can engage in several unique protein-pro...
Conserved hydrophobic core residues are indicated by *, and totally conserved residues by #. The blu...
<p><b>A</b>) Ribbon representation of an alignment of K48-linked diubiquitin structures. The proxima...