WWP2: Difference between revisions
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<StructureSection load='5TJ7' size='350' side='right' caption="WWP2 Ubiquitin Ligase Chimeric Structure (PDB entry [[5TJ7]]). The 2,3-linker (red) connects the WW2 domain (yellow) to the WW3 domain. | <StructureSection load='5TJ7' size='350' side='right' caption="WWP2 Ubiquitin Ligase Chimeric Structure (PDB entry [[5TJ7]]). The 2,3-linker (red) connects the WW2 domain (yellow) to the WW3 domain. The hinge (magenta) connects the C-terminal lobe (green) and N-terminal lobe (silver) of the HECT domain." scene="84/848928/Overallcolored/13"> | ||
==Introduction== | ==Introduction== | ||
'''WWP2''' (WW domain-containing protein 2) is a type of [[ubiquitin protein ligase]]. Ubiquitination can serve as a signal for degradation, lead to translocation within the cell, and result in altered activity and altered protein-protein interactions. The ubiquitination pathway comprises of ubiquitin-activating (E1), ubiquitin-conjugating (E2) and ubiquitin-ligating (E3) enzymes. WWP2 is a member of the HECT ('''H'''omologous to the '''E'''6-AP '''C'''arboxyl '''T'''erminus) E3 Ligase class of enzymes. HECT E3 Ligases accept a [[ubiquitin]] molecule from E2 enzymes and transfer the ubiquitin to a Lysine residue in the target signaling molecule or transcription factor. | '''WWP2''' (WW domain-containing protein 2) is a type of [[ubiquitin protein ligase]]. Ubiquitination can serve as a signal for degradation, lead to translocation within the cell, and result in altered activity and altered protein-protein interactions. The ubiquitination pathway comprises of ubiquitin-activating (E1), ubiquitin-conjugating (E2) and ubiquitin-ligating (E3) enzymes. WWP2 is a member of the HECT ('''H'''omologous to the '''E'''6-AP '''C'''arboxyl '''T'''erminus) E3 Ligase class of enzymes. HECT E3 Ligases accept a [[ubiquitin]] molecule from E2 enzymes and transfer the ubiquitin to a Lysine residue in the target signaling molecule or transcription factor. | ||
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==Structure== | ==Structure== | ||
[Image:WWP2 Scheme from paper fig 1A top.png|300px|right|thumb| WWP2 Scheme without C2 Domain]] | |||
[[Image:WWP2 Scheme from paper D3.png|300px|right|thumb| WWP2 Scheme WW2-2,3-linker-HECT]] | [[Image:WWP2 Scheme from paper D3.png|300px|right|thumb| WWP2 Scheme WW2-2,3-linker-HECT]] | ||
Full-length WWP2 consists of an amino-terminal C2 domain, four WW domains (labeled WW1-WW4), and a carboxy-terminal HECT domain. WW domains are one of the smallest studied protein modules, consisting of less than 40 amino acids, fold into three-stranded beta-sheets. They are characterized by two highly conserved <scene name='84/848928/Trpsinww2/2'>Trp residues</scene> positioned 20-22 amino acids apart and a high affinity for proline-rich motifs. Linkers of varying length and secondary structure connect the C2 domain to WW1, WW1 to WW2, WW2 to WW3, WW3 to WW4, and WW4 to the HECT domain. A chimeric <scene name='84/848928/Overallcolored/12'>structure</scene> of WWP2 consisting of the <scene name='84/848928/Ww2_domain/8'>WW2 domain</scene>, the WW2-WW3 linker (<scene name='84/848928/Linkeronly/1'>2,3-linker</scene>), and the HECT domain is shown on the right. | Full-length WWP2 consists of an amino-terminal C2 domain, four WW domains (labeled WW1-WW4), and a carboxy-terminal HECT domain. WW domains are one of the smallest studied protein modules, consisting of less than 40 amino acids, fold into three-stranded beta-sheets. They are characterized by two highly conserved <scene name='84/848928/Trpsinww2/2'>Trp residues</scene> positioned 20-22 amino acids apart and a high affinity for proline-rich motifs. Linkers of varying length and secondary structure connect the C2 domain to WW1, WW1 to WW2, WW2 to WW3, WW3 to WW4, and WW4 to the HECT domain. A chimeric <scene name='84/848928/Overallcolored/12'>structure</scene> of WWP2 consisting of the <scene name='84/848928/Ww2_domain/8'>WW2 domain</scene>, the WW2-WW3 linker (<scene name='84/848928/Linkeronly/1'>2,3-linker</scene>), and the HECT domain is shown on the right. | ||
