1an4
From Proteopedia
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| - | [[Image:1an4.jpg|left|200px]] | + | [[Image:1an4.jpg|left|200px]] |
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| - | '''STRUCTURE AND FUNCTION OF THE B/HLH/Z DOMAIN OF USF''' | + | {{Structure |
| + | |PDB= 1an4 |SIZE=350|CAPTION= <scene name='initialview01'>1an4</scene>, resolution 2.900Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''STRUCTURE AND FUNCTION OF THE B/HLH/Z DOMAIN OF USF''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AN4 is a [ | + | 1AN4 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=1AN4 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure and function of the b/HLH/Z domain of USF., Ferre-D'Amare AR, Pognonec P, Roeder RG, Burley SK, EMBO J. 1994 Jan 1;13(1):180-9. PMID:[http:// | + | Structure and function of the b/HLH/Z domain of USF., Ferre-D'Amare AR, Pognonec P, Roeder RG, Burley SK, EMBO J. 1994 Jan 1;13(1):180-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8306960 8306960] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''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 09:59:49 2008'' |
Revision as of 07:59, 20 March 2008
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| , resolution 2.900Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE AND FUNCTION OF THE B/HLH/Z DOMAIN OF USF
Contents |
Overview
The basic/helix-loop-helix/leucine zipper (b/HLH/Z) transcription factor upstream stimulatory factor (USF) and its isolated DNA binding domain undergo a random coil to alpha-helix folding transition on recognizing their cognate DNA. The USF b/HLH cocrystal structure resembles the structure of the b/HLH/Z domain of the homologous protein Max and reveals (i) that the truncated, b/HLH DNA binding domain homodimerizes, forming a parallel, left-handed four-helix bundle, and (ii) that the basic region becomes alpha-helical on binding to the major groove of the DNA sequence CACGTG. Hydrodynamic measurements show that the b/HLH/Z DNA binding domain of USF exists as a bivalent homotetramer. This tetramer forms at the USF physiological intranuclear concentration, and depends on the integrity of the leucine zipper motif. The ability to bind simultaneously to two independent sites suggests a role in DNA looping for the b/HLH/Z and Myc-related families of eukaryotic transcription factors.
Disease
Known diseases associated with this structure: Hyperlipidemia, familial combined, susceptibility to OMIM:[191523]
About this Structure
1AN4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure and function of the b/HLH/Z domain of USF., Ferre-D'Amare AR, Pognonec P, Roeder RG, Burley SK, EMBO J. 1994 Jan 1;13(1):180-9. PMID:8306960
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