1kql

<StructureSection load='1kql' size='340' side='right' caption='[[1kql]], [[Resolution|resolution]] 2.70&Aring;' scene=''>

<table><tr><td colspan='2'>[[1kql]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KQL FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kql OCA], [http://pdbe.org/1kql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kql RCSB], [http://www.ebi.ac.uk/pdbsum/1kql PDBsum]</span></td></tr>

[[http://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'.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kq/1kql_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

Contraction in striated and cardiac muscles is regulated by the motions of a Ca(2+)-sensitive tropomyosin/troponin switch. In contrast, troponin is absent in other muscle types and in nonmuscle cells, and actomyosin regulation is myosin-linked. Here we report an unusual crystal structure at 2.7 A of the C-terminal 31 residues of rat striated-muscle alpha-tropomyosin (preceded by a fragment of the GCN4 leucine zipper). The C-terminal 22 residues (263-284) of the structure do not form a two-stranded alpha-helical coiled coil as does the rest of the molecule, but here the alpha-helices splay apart and are stabilized by the formation of a tail-to-tail dimer with a symmetry-related molecule. The site of splaying involves a small group of destabilizing core residues that is present only in striated muscle tropomyosin isoforms. These results reveal a specific recognition site for troponin T and clarify the physical basis for the unique regulatory mechanism of striated muscles.

The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site.,Li Y, Mui S, Brown JH, Strand J, Reshetnikova L, Tobacman LS, Cohen C Proc Natl Acad Sci U S A. 2002 May 28;99(11):7378-83. PMID:12032291<ref>PMID:12032291</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1kql" style="background-color:#fffaf0;"></div>

*[[Gcn4|Gcn4]]

*[[Tropomyosin|Tropomyosin]]

[[Category: Atcc 18824]]

[[Category: Brown, J H]]

[[Category: Cohen, C]]

[[Category: Li, Y]]

[[Category: Mui, S]]

[[Category: Reshetnikova, L]]

[[Category: Strand, J]]

[[Category: Tobacman, L S]]

[[Category: Contractile protein]]

[[Category: Four-helix bundle]]

[[Category: Tropomyosin]]