1v66
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1v66.gif|left|200px]] | + | [[Image:1v66.gif|left|200px]] |
| - | + | ||
| - | '''Solution structure of human p53 binding domain of PIAS-1''' | + | {{Structure |
| + | |PDB= 1v66 |SIZE=350|CAPTION= <scene name='initialview01'>1v66</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of human p53 binding domain of PIAS-1''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1V66 is a [ | + | 1V66 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V66 OCA]. |
==Reference== | ==Reference== | ||
| - | NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers., Okubo S, Hara F, Tsuchida Y, Shimotakahara S, Suzuki S, Hatanaka H, Yokoyama S, Tanaka H, Yasuda H, Shindo H, J Biol Chem. 2004 Jul 23;279(30):31455-61. Epub 2004 May 8. PMID:[http:// | + | NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers., Okubo S, Hara F, Tsuchida Y, Shimotakahara S, Suzuki S, Hatanaka H, Yokoyama S, Tanaka H, Yasuda H, Shindo H, J Biol Chem. 2004 Jul 23;279(30):31455-61. Epub 2004 May 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15133049 15133049] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 27: | Line 36: | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:41:23 2008'' |
Revision as of 12:41, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of human p53 binding domain of PIAS-1
Overview
A member of the PIAS (protein inhibitor of activated STAT) family of proteins, PIAS1, have been reported to serve as an E3-type SUMO ligase for tumor suppressor p53 and its own. It also was proposed that the N-terminal domain of PIAS1 interacts with DNA as well as p53. Extensive biochemical studies have been devoted recently to understand sumoylations and its biological implications, whereas the structural aspects of the PIAS family and the mechanism of its interactions with various factors are less well known to date. In this study, the three-dimensional structure of the N-terminal domain (residues 1-65) of SUMO ligase PIAS1 was determined by NMR spectroscopy. The structure revealed a unique four-helix bundle with a topology of an up-down-extended loop-down-up, a part of which the helix-extended loop-helix represented the SAP (SAF-A/B, Acinus, and PIAS) motif. Thus, this N-terminal domain may be referred to as a four-helix SAP domain. The glutathione S-transferase pull-down assay demonstrated that this domain possesses a binding ability to tumor suppressor p53, a target protein for sumoylation by PIAS1, whereas gel mobility assays showed that it has a strong affinity toward A/T-rich DNA. An NMR analysis of the four-helix SAP domain complexed with the 16-bp-long DNA demonstrated that one end of the four-helix bundle is the binding site and may fit into the minor groove of DNA. The three-dimensional structure and its binding duality are discussed in conjunction with the biological functions of PIAS1 as a SUMO ligase.
About this Structure
1V66 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers., Okubo S, Hara F, Tsuchida Y, Shimotakahara S, Suzuki S, Hatanaka H, Yokoyama S, Tanaka H, Yasuda H, Shindo H, J Biol Chem. 2004 Jul 23;279(30):31455-61. Epub 2004 May 8. PMID:15133049
Page seeded by OCA on Thu Mar 20 14:41:23 2008
Categories: Homo sapiens | Single protein | Hara, F. | Hatanaka, H. | Okubo, S. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shimotakahara, S. | Shindo, H. | Suzuki, S. | Tanaka, H. | Tsuchida, Y. | Yasuda, H. | Yokoyama, S. | Four helix bundle | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
