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1an4

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[[Image:1an4.jpg|left|200px]]<br /><applet load="1an4" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1an4, resolution 2.900&Aring;" />
 
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'''STRUCTURE AND FUNCTION OF THE B/HLH/Z DOMAIN OF USF'''<br />
 
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==Overview==
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==STRUCTURE AND FUNCTION OF THE B/HLH/Z DOMAIN OF USF==
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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.
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<StructureSection load='1an4' size='340' side='right'caption='[[1an4]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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==Disease==
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<table><tr><td colspan='2'>[[1an4]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AN4 FirstGlance]. <br>
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Known diseases associated with this structure: Hyperlipidemia, familial combined, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191523 191523]]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1an4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1an4 OCA], [https://pdbe.org/1an4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1an4 RCSB], [https://www.ebi.ac.uk/pdbsum/1an4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1an4 ProSAT]</span></td></tr>
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==About this Structure==
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</table>
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1AN4 is a [http://en.wikipedia.org/wiki/Single_protein 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].
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== Disease ==
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[https://www.uniprot.org/uniprot/USF1_HUMAN USF1_HUMAN] Genetic variations in USF1 are associated with hyperlipidemia combined type 1 (HYPLIP1) [MIM:[https://omim.org/entry/602491 602491]; also known as familial combined hyperlipidemia type 1 (FCHL1). HYPLIP1 is characterized by elevated levels of serum total cholesterol, triglycerides or both, and is observed in about 20% of individuals with premature coronary heart disease.<ref>PMID:14991056</ref>
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==Reference==
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== Function ==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8306960 8306960]
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[https://www.uniprot.org/uniprot/USF1_HUMAN USF1_HUMAN] Transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/an/1an4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1an4 ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Amare, A R.Ferre-D.]]
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[[Category: Burley SK]]
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[[Category: Burley, S K.]]
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[[Category: Ferre-D'Amare AR]]
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[[Category: Pognonec, P.]]
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[[Category: Pognonec P]]
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[[Category: Roeder, R G.]]
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[[Category: Roeder RG]]
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[[Category: double helix]]
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[[Category: overhanging base]]
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[[Category: protein-dna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:18 2008''
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Current revision

STRUCTURE AND FUNCTION OF THE B/HLH/Z DOMAIN OF USF

PDB ID 1an4

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