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1cok
From Proteopedia
| 1cok, 18 NMR models () | |||||||||
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| Domains: | SAM_2 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
STRUCTURE OF THE C-TERMINAL DOMAIN OF P73
p73 and p63 are two recently cloned genes with homology to the tumor suppressor p53, whose protein product is a key transcriptional regulator of genes involved in cell cycle arrest and apoptosis. While all three proteins share conserved transcriptional activation, DNA-binding and oligomerization domains, p73 and p63 have an additional conserved C-terminal region. We have determined the three-dimensional solution structure of this conserved C-terminal domain of human p73. The structure reveals a small five-helix bundle with striking similarity to the SAM (sterile alpha motif) domains of two ephrin receptor tyrosine kinases. The SAM domain is a putative protein-protein interaction domain found in a variety of cytoplasmic signaling proteins and has been shown to form both homo- and hetero-oligomers. However, the SAM-like C-terminal domains of p73 and p63 are monomeric and do not interact with one another, suggesting that this domain may interact with additional, as yet uncharacterized proteins in a signaling and/or regulatory role.
Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain., Chi SW, Ayed A, Arrowsmith CH, EMBO J. 1999 Aug 16;18(16):4438-45. PMID:10449409
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1COK is a 1 chain structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
- Chi SW, Ayed A, Arrowsmith CH. Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain. EMBO J. 1999 Aug 16;18(16):4438-45. PMID:10449409 doi:10.1093/emboj/18.16.4438
Page seeded by OCA on Tue Feb 17 06:54:50 2009
