2qfj
From Proteopedia
(New page: 200px<br /><applet load="2qfj" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qfj, resolution 2.10Å" /> '''Crystal Structure of...) |
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| - | [[Image:2qfj.jpg|left|200px]] | + | [[Image:2qfj.jpg|left|200px]] |
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| - | '''Crystal Structure of First Two RRM Domains of FIR Bound to ssDNA from a Portion of FUSE''' | + | {{Structure |
| + | |PDB= 2qfj |SIZE=350|CAPTION= <scene name='initialview01'>2qfj</scene>, resolution 2.10Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= FIR, SIAHBP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
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| + | '''Crystal Structure of First Two RRM Domains of FIR Bound to ssDNA from a Portion of FUSE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2QFJ is a [ | + | 2QFJ is a [[Protein complex]] structure of sequences 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=2QFJ OCA]. |
==Reference== | ==Reference== | ||
| - | Dimerization of FIR upon FUSE DNA binding suggests a mechanism of c-myc inhibition., Crichlow GV, Zhou H, Hsiao HH, Frederick KB, Debrosse M, Yang Y, Folta-Stogniew EJ, Chung HJ, Fan C, De la Cruz EM, Levens D, Lolis E, Braddock D, EMBO J. 2008 Jan 9;27(1):277-89. Epub 2007 Dec 6. PMID:[http:// | + | Dimerization of FIR upon FUSE DNA binding suggests a mechanism of c-myc inhibition., Crichlow GV, Zhou H, Hsiao HH, Frederick KB, Debrosse M, Yang Y, Folta-Stogniew EJ, Chung HJ, Fan C, De la Cruz EM, Levens D, Lolis E, Braddock D, EMBO J. 2008 Jan 9;27(1):277-89. Epub 2007 Dec 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18059478 18059478] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: transcription repressor/dna complex]] | [[Category: transcription repressor/dna complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:25:22 2008'' |
Revision as of 16:25, 20 March 2008
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| , resolution 2.10Å | |||||||
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| Gene: | FIR, SIAHBP1 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of First Two RRM Domains of FIR Bound to ssDNA from a Portion of FUSE
Overview
c-myc is essential for cell homeostasis and growth but lethal if improperly regulated. Transcription of this oncogene is governed by the counterbalancing forces of two proteins on TFIIH--the FUSE binding protein (FBP) and the FBP-interacting repressor (FIR). FBP and FIR recognize single-stranded DNA upstream of the P1 promoter, known as FUSE, and influence transcription by oppositely regulating TFIIH at the promoter site. Size exclusion chromatography coupled with light scattering reveals that an FIR dimer binds one molecule of single-stranded DNA. The crystal structure confirms that FIR binds FUSE as a dimer, and only the N-terminal RRM domain participates in nucleic acid recognition. Site-directed mutations of conserved residues in the first RRM domain reduce FIR's affinity for FUSE, while analogous mutations in the second RRM domain either destabilize the protein or have no effect on DNA binding. Oppositely oriented DNA on parallel binding sites of the FIR dimer results in spooling of a single strand of bound DNA, and suggests a mechanism for c-myc transcriptional control.
About this Structure
2QFJ is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Dimerization of FIR upon FUSE DNA binding suggests a mechanism of c-myc inhibition., Crichlow GV, Zhou H, Hsiao HH, Frederick KB, Debrosse M, Yang Y, Folta-Stogniew EJ, Chung HJ, Fan C, De la Cruz EM, Levens D, Lolis E, Braddock D, EMBO J. 2008 Jan 9;27(1):277-89. Epub 2007 Dec 6. PMID:18059478
Page seeded by OCA on Thu Mar 20 18:25:22 2008
