1z60

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[[Image:1z60.gif|left|200px]]
[[Image:1z60.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1z60", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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{{STRUCTURE_1z60| PDB=1z60 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z60 OCA], [http://www.ebi.ac.uk/pdbsum/1z60 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1z60 RCSB]</span>
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'''Solution structure of the carboxy-terminal domain of human TFIIH P44 subunit'''
'''Solution structure of the carboxy-terminal domain of human TFIIH P44 subunit'''
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==About this Structure==
==About this Structure==
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1Z60 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1E53. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z60 OCA].
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1Z60 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1e53 1e53]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z60 OCA].
==Reference==
==Reference==
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[[Category: Poterszman, A.]]
[[Category: Poterszman, A.]]
[[Category: Wasielewski, E.]]
[[Category: Wasielewski, E.]]
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[[Category: basic transcription factor]]
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[[Category: Basic transcription factor]]
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[[Category: ring finger]]
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[[Category: Ring finger]]
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[[Category: zinc binding protein]]
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[[Category: Zinc binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:12:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:29:33 2008''
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Revision as of 14:12, 3 May 2008

Template:STRUCTURE 1z60

Solution structure of the carboxy-terminal domain of human TFIIH P44 subunit


Overview

The human general transcription factor TFIIH is involved in both transcription and DNA nucleotide excision repair. Among the 10 subunits of the complex, p44 subunit plays a crucial role in both mechanisms. Its N-terminal domain interacts with the XPD helicase, whereas its C-terminal domain is involved specifically in the promoter escape activity. By mutating an exposed and non-conserved cysteine residue into a serine, we produced a soluble mutant of p44-(321-395) suitable for solution structure determination. The domain adopts a C4C4 RING domain structure with sequential organization of beta-strands that is related to canonical RING domains by a circular permutation of the beta-sheet elements. Analysis of the molecular surface and mutagenesis experiments suggests that the binding of p44-(321-395) to TFIIH p34 subunit is not mediated by electrostatic interactions and, thus, differs from previously reported interaction mechanisms involving RING domains.

About this Structure

1Z60 is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1e53. Full crystallographic information is available from OCA.

Reference

Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions., Kellenberger E, Dominguez C, Fribourg S, Wasielewski E, Moras D, Poterszman A, Boelens R, Kieffer B, J Biol Chem. 2005 May 27;280(21):20785-92. Epub 2005 Mar 24. PMID:15790571 Page seeded by OCA on Sat May 3 17:12:50 2008

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