<div><p>(A) MDM2 peptide (red) binds to the same surface groove as the p53 peptide (magenta). Residues from MDM2 and p53 are shown in yellow and green, respectively.</p> <p>(B) Superposition of three HAUSP-binding peptides derived from MDM2 (red), p53 (magenta), and EBNA1 (green). The HAUSP TRAF-like domain is shown in a transparent surface representation, with critical residues shown in brown.</p> <p>(C) Structural alignment of HAUSP-binding peptides reveals a consensus sequence. The HAUSP surface groove (in a transparent surface representation) for binding to the consensus tetrapeptide is shown in the left panel. The consensus sequence is shown in the right panel.</p></div
(A) Linear diagram of the HAP2 primary structure indicating the positions of the signal peptide (“S”...
Mdm2 is a major negative regulator of the tumor suppressor p53 protein, a protein that plays a cruci...
<p>Only the tryptophan residue of each peptide (with 6-chloro group shown in green for M011) and ami...
<div><p>(A) Overall structure of the HAUSP TRAF-like domain bound to MDM2 peptide is shown in a ribb...
<div><p>(A) Structure of the HAUSP TRAF-like domain in a ribbon diagram (left) and a surface represe...
<div><p>(A) The TRAF-like domain of HAUSP is responsible for binding to MDM2. Various HAUSP fragment...
<p>(<b>A</b>) superpositions of MIP-MDM2 fusion (PDB ID = 2RUH), DI:MDM2 (3G03), PMI:MDM2 (3EQS), an...
<div><p>(A) Structure of a HAUSP fragment (residues 53–560) that contains both the substrate-binding...
<p>Shaded residues are the conserved interacting residues (F19, W23 and L26) derived from p53. Xr an...
<p><b>A.</b> Ligand-free MDM2 (1z1m, green) with p53 peptide (cyan) from the bound structure (3v3b)....
<p>(<b>A</b>) The hydrophobic groove, depicted in <i>yellow</i>, is present between domains II and I...
<p>The secondary structure is depicted above the primary sequence. Red arrows above the sequences co...
<p>(<b>A</b>) A network of hydrogen bonding and hydrophobic interactions formed by the phosphorylate...
MDM2 is a negative regulator of p53. The N terminal domain of MDM2 interacts with a helical region o...
<p>Structure superposition of the binding sites of murine I-Ab (PBD code: 1MUJ) and human HLA-DR4 (P...
(A) Linear diagram of the HAP2 primary structure indicating the positions of the signal peptide (“S”...
Mdm2 is a major negative regulator of the tumor suppressor p53 protein, a protein that plays a cruci...
<p>Only the tryptophan residue of each peptide (with 6-chloro group shown in green for M011) and ami...
<div><p>(A) Overall structure of the HAUSP TRAF-like domain bound to MDM2 peptide is shown in a ribb...
<div><p>(A) Structure of the HAUSP TRAF-like domain in a ribbon diagram (left) and a surface represe...
<div><p>(A) The TRAF-like domain of HAUSP is responsible for binding to MDM2. Various HAUSP fragment...
<p>(<b>A</b>) superpositions of MIP-MDM2 fusion (PDB ID = 2RUH), DI:MDM2 (3G03), PMI:MDM2 (3EQS), an...
<div><p>(A) Structure of a HAUSP fragment (residues 53–560) that contains both the substrate-binding...
<p>Shaded residues are the conserved interacting residues (F19, W23 and L26) derived from p53. Xr an...
<p><b>A.</b> Ligand-free MDM2 (1z1m, green) with p53 peptide (cyan) from the bound structure (3v3b)....
<p>(<b>A</b>) The hydrophobic groove, depicted in <i>yellow</i>, is present between domains II and I...
<p>The secondary structure is depicted above the primary sequence. Red arrows above the sequences co...
<p>(<b>A</b>) A network of hydrogen bonding and hydrophobic interactions formed by the phosphorylate...
MDM2 is a negative regulator of p53. The N terminal domain of MDM2 interacts with a helical region o...
<p>Structure superposition of the binding sites of murine I-Ab (PBD code: 1MUJ) and human HLA-DR4 (P...
(A) Linear diagram of the HAP2 primary structure indicating the positions of the signal peptide (“S”...
Mdm2 is a major negative regulator of the tumor suppressor p53 protein, a protein that plays a cruci...
<p>Only the tryptophan residue of each peptide (with 6-chloro group shown in green for M011) and ami...