From Proteopedia
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| - | [[Image:1gji.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1gji| PDB=1gji | SCENE= }} | | {{STRUCTURE_1gji| PDB=1gji | SCENE= }} |
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| - | '''Crystal structure of c-Rel bound to DNA'''
| + | ===Crystal structure of c-Rel bound to DNA=== |
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| - | ==Overview==
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| - | BACKGROUND: The proto-oncogene product c-Rel is a Rel/NF-kappaB family transcription factor that plays a critical role in lymphoid cell development and mediates CD28-induced expression of interleukin 2 (IL-2). The CD28 response element (CD28RE) in the IL-2 enhancer is nonameric and similar to the kappaB DNA target sites recognized by p65 homodimers. RESULTS: We have determined and refined the X-ray crystal structure of the c-Rel homodimer complexed to the CD28RE DNA site, 5'-AGAAATTCC-3', to 2.85 A resolution. The c-Rel homodimer binds CD28RE in a mode similar to that observed in the p65/IL-8 kappaB crystallographic complex. Binding studies reveal that the c-Rel homodimer recognizes the CD28RE with higher affinity as compared to other canonical kappaB sequences despite the nonconsensus A:T base pair at the 5' end of the CD28RE. Preferential recognition of the CD28RE by c-Rel results from the direct contacts between the protein and the DNA as well as intrasubunit interactions between the beta(f)-beta(g) loop in the dimerization domain and the DNA-contacting loop L1 of the N-terminal domain. Not only do these loops have different conformations in other Rel/DNA crystallographic complexes, but they also contain two of the five oncogenic point mutations found in v-Rel. CONCLUSIONS: The current structure indicates that a non-DNA-contacting loop in the dimerization domain and the DNA-contacting loop L1 may play critical roles in defining affinity and specificity. Two amino acid changes in these segments may account for the differential DNA binding by v-Rel as compared to that of c-Rel.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11587641}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11587641 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11587641}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Nf-kb/dna complex]] | | [[Category: Nf-kb/dna complex]] |
| | [[Category: Transcription factor]] | | [[Category: Transcription factor]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:39:12 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:23:42 2008'' |
Revision as of 02:23, 1 July 2008
Template:STRUCTURE 1gji
Crystal structure of c-Rel bound to DNA
Template:ABSTRACT PUBMED 11587641
About this Structure
1GJI is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of proto-oncogene product c-Rel bound to the CD28 response element of IL-2., Huang DB, Chen YQ, Ruetsche M, Phelps CB, Ghosh G, Structure. 2001 Aug;9(8):669-78. PMID:11587641
Page seeded by OCA on Tue Jul 1 05:23:42 2008
