1j4w
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1j4w.gif|left|200px]] | + | [[Image:1j4w.gif|left|200px]] |
| - | + | ||
| - | '''COMPLEX OF THE KH3 and KH4 DOMAINS OF FBP WITH A SINGLE_STRANDED 29mer DNA OLIGONUCLEOTIDE FROM THE FUSE ELEMENT OF THE C-MYC ONCOGENE''' | + | {{Structure |
| + | |PDB= 1j4w |SIZE=350|CAPTION= <scene name='initialview01'>1j4w</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''COMPLEX OF THE KH3 and KH4 DOMAINS OF FBP WITH A SINGLE_STRANDED 29mer DNA OLIGONUCLEOTIDE FROM THE FUSE ELEMENT OF THE C-MYC ONCOGENE''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1J4W is a [ | + | 1J4W 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=1J4W OCA]. |
==Reference== | ==Reference== | ||
| - | Structure and dynamics of KH domains from FBP bound to single-stranded DNA., Braddock DT, Louis JM, Baber JL, Levens D, Clore GM, Nature. 2002 Feb 28;415(6875):1051-6. PMID:[http:// | + | Structure and dynamics of KH domains from FBP bound to single-stranded DNA., Braddock DT, Louis JM, Baber JL, Levens D, Clore GM, Nature. 2002 Feb 28;415(6875):1051-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11875576 11875576] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 21: | Line 30: | ||
[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''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 11:58:55 2008'' |
Revision as of 09:59, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COMPLEX OF THE KH3 and KH4 DOMAINS OF FBP WITH A SINGLE_STRANDED 29mer DNA OLIGONUCLEOTIDE FROM THE FUSE ELEMENT OF THE C-MYC ONCOGENE
Overview
Gene regulation can be tightly controlled by recognition of DNA deformations that are induced by stress generated during transcription. The KH domains of the FUSE-binding protein (FBP), a regulator of c-myc expression, bind in vivo and in vitro to the single-stranded far-upstream element (FUSE), 1,500 base pairs upstream from the c-myc promoter. FBP bound to FUSE acts through TFIIH at the promoter. Here we report the solution structure of a complex between the KH3 and KH4 domains of FBP and a 29-base single-stranded DNA from FUSE. The KH domains recognize two sites, 9-10 bases in length, separated by 5 bases, with KH4 bound to the 5' site and KH3 to the 3' site. The central portion of each site comprises a tetrad of sequence 5'd-ATTC for KH4 and 5'd-TTTT for KH3. Dynamics measurements show that the two KH domains bind as articulated modules to single-stranded DNA, providing a flexible framework with which to recognize transient, moving targets.
About this Structure
1J4W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure and dynamics of KH domains from FBP bound to single-stranded DNA., Braddock DT, Louis JM, Baber JL, Levens D, Clore GM, Nature. 2002 Feb 28;415(6875):1051-6. PMID:11875576
Page seeded by OCA on Thu Mar 20 11:58:55 2008
