1svc: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1svc.gif|left|200px]] | [[Image:1svc.gif|left|200px]] | ||
'''NFKB P50 HOMODIMER BOUND TO DNA''' | {{Structure | ||
|PDB= 1svc |SIZE=350|CAPTION= <scene name='initialview01'>1svc</scene>, resolution 2.600Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''NFKB P50 HOMODIMER BOUND TO DNA''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1SVC is a [ | 1SVC 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=1SVC OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the NF-kappa B p50 homodimer bound to DNA., Muller CW, Rey FA, Sodeoka M, Verdine GL, Harrison SC, Nature. 1995 Jan 26;373(6512):311-7. PMID:[http:// | Structure of the NF-kappa B p50 homodimer bound to DNA., Muller CW, Rey FA, Sodeoka M, Verdine GL, Harrison SC, Nature. 1995 Jan 26;373(6512):311-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7830764 7830764] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 23: | Line 32: | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
''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 14:10:04 2008'' | ||
Revision as of 12:10, 20 March 2008
| |||||||||||||
| 1svc, resolution 2.600Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
NFKB P50 HOMODIMER BOUND TO DNA
Overview
The structure of a large fragment of the p50 subunit of the human transcription factor NF-kappa B, bound as a homodimer to DNA, reveals that the Rel-homology region has two beta-barrel domains that grip DNA in the major groove. Both domains contact the DNA backbone. The amino-terminal specificity domain contains a recognition loop that interacts with DNA bases; the carboxy-terminal dimerization domain bears the site of I-kappa B interaction. The folds of these domains are related to immunoglobulin-like modules. The amino-terminal domain also resembles the core domain of p53.
About this Structure
1SVC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the NF-kappa B p50 homodimer bound to DNA., Muller CW, Rey FA, Sodeoka M, Verdine GL, Harrison SC, Nature. 1995 Jan 26;373(6512):311-7. PMID:7830764
Page seeded by OCA on Thu Mar 20 14:10:04 2008