1nd7

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[[Image:1nd7.jpg|left|200px]]
[[Image:1nd7.jpg|left|200px]]
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{{Structure
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|PDB= 1nd7 |SIZE=350|CAPTION= <scene name='initialview01'>1nd7</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1nd7", creates the "Structure Box" on the page.
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|GENE= WWP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1nd7| PDB=1nd7 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nd7 OCA], [http://www.ebi.ac.uk/pdbsum/1nd7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nd7 RCSB]</span>
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'''Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain E3 Ligase'''
'''Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain E3 Ligase'''
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[[Category: Verdecia, M A.]]
[[Category: Verdecia, M A.]]
[[Category: Wells, N J.]]
[[Category: Wells, N J.]]
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[[Category: e3]]
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[[Category: E3]]
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[[Category: hect]]
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[[Category: Hect]]
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[[Category: ligase]]
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[[Category: Ligase]]
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[[Category: ubiquitin]]
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[[Category: Ubiquitin]]
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[[Category: wwp1]]
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[[Category: Wwp1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:23:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:28:51 2008''
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Revision as of 23:23, 2 May 2008

Image:1nd7.jpg

Template:STRUCTURE 1nd7

Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain E3 Ligase


Overview

Ubiquitin ligases (E3) select proteins for ubiquitylation, a modification that directs altered subcellular trafficking and/or degradation of the target protein. HECT domain E3 ligases not only recognize, but also directly catalyze, ligation of ubiquitin to their protein substrates. The crystal structure of the HECT domain of the human ubiquitin ligase WWP1/AIP5 maintains a two-lobed structure like the HECT domain of the human ubiquitin ligase E6AP. While the individual N and C lobes of WWP1 possess very similar folds to those of E6AP, the organization of the two lobes relative to one another is different from E6AP due to a rotation about a polypeptide hinge linking the N and C lobes. Mutational analyses suggest that a range of conformations achieved by rotation about this hinge region is essential for catalytic activity.

About this Structure

1ND7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase., Verdecia MA, Joazeiro CA, Wells NJ, Ferrer JL, Bowman ME, Hunter T, Noel JP, Mol Cell. 2003 Jan;11(1):249-59. PMID:12535537 Page seeded by OCA on Sat May 3 02:23:39 2008

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