3ck4: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:3ck4.jpg|left|200px]]
-<!--
+==A heterospecific leucine zipper tetramer==
-The line below this paragraph, containing "STRUCTURE_3ck4", creates the "Structure Box" on the page.
+<StructureSection load='3ck4' size='340' side='right'caption='[[3ck4]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3ck4]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CK4 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-{{STRUCTURE_3ck4|  PDB=3ck4  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ck4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ck4 OCA], [https://pdbe.org/3ck4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ck4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ck4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ck4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GCN4_YEAST GCN4_YEAST] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Protein-protein interactions play an essential role in the assembly of the macromolecular complexes that form functional networks and control cellular behavior. Elucidating principles of molecular recognition governing potentially complex interfaces is a challenging goal for structural and systems biology. Extensive studies of alpha-helical coiled coils have provided fundamental insight into the determinants of one seemingly tractable class of oligomeric protein interfaces. We report here that two different valine-containing mutants of the GCN4 leucine zipper that fold individually as four-stranded coiled coils associate preferentially in mixtures to form an antiparallel, heterotetrameric structure. X-ray crystallographic analysis reveals that the coinciding hydrophobic interfaces of the hetero- and homotetramers differ in detail, thereby controlling their partnering and structural specificity. Equilibrium disulfide exchange and thermal denaturation experiments show that the 50-fold preference for heterospecificity is determined by interfacial van der Waals interactions and hydrophobicity. Parallel studies of two alanine-containing variants confirm the above-mentioned interpretation of the basis and mechanism of this heterospecificity. Our results suggest that coiled-coil recognition is an inherently geometric process in which heterotypic interaction specificity derives from a complementarity of both shape and chemistry.
-===A heterospecific leucine zipper tetramer===
+A heterospecific leucine zipper tetramer.,Deng Y, Liu J, Zheng Q, Li Q, Kallenbach NR, Lu M Chem Biol. 2008 Sep 22;15(9):908-19. PMID:18804028<ref>PMID:18804028</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3ck4" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_18804028}}, adds the Publication Abstract to the page
+*[[Gcn4 3D Structures|Gcn4 3D Structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 18804028 is the PubMed ID number.
+*[[Gnc4 3D Structures|Gnc4 3D Structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_18804028}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-CK4 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CK4 OCA].
+[[Category: Large Structures]]
-==Reference==
-A heterospecific leucine zipper tetramer., Deng Y, Liu J, Zheng Q, Li Q, Kallenbach NR, Lu M, Chem Biol. 2008 Sep 22;15(9):908-19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18804028 18804028]
-[[Category: Protein complex]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Liu, J.]]
+[[Category: Liu J]]
-[[Category: Activator]]
-[[Category: Amino-acid biosynthesis]]
-[[Category: Anti-parallel tetramer]]
-[[Category: Coiled coil]]
-[[Category: Dna-binding]]
-[[Category: Heterospecific interaction]]
-[[Category: Nucleus]]
-[[Category: Phosphoprotein]]
-[[Category: Protein binding]]
-[[Category: Protein complex]]
-[[Category: Transcription]]
-[[Category: Transcription regulation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct  8 09:27:40 2008''