1tul

<StructureSection load='1tul' size='340' side='right' caption='[[1tul]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[1tul]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acmnpv Acmnpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TUL 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=1tul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tul OCA], [http://pdbe.org/1tul PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tul RCSB], [http://www.ebi.ac.uk/pdbsum/1tul PDBsum]</span></td></tr>

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

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== Publication Abstract from PubMed ==

Myosin light-chain kinase is responsible for the phosphorylation of myosin in smooth muscle cells. In some tissue types, the C-terminal portion of this large enzyme is expressed as an independent protein and has been given the name telokin. Recently, an antibody directed against telokin was found to interact with a protein derived from the baculovirus Autographa californica nuclear polyhedrosis virus. This protein was biochemically characterized and given the name TLP20 for telokin-like protein of 20 000 molecular weight. The amino-acid sequence of TLP20 was determined on the basis of a cDNA clone and subsequent alignment searches failed to reveal any homology to telokin or to other known proteins. The three-dimensional structure of a proteolytic portion of TLP20 is reported here. Crystals employed in the investigation were grown from ammonium sulfate solutions at pH 6.0 and belonged to the space group P2(1)3 with unit-cell dimensions of a = b = c = 76.3 A and one molecule per asymmetric unit. The structure was determined by multiple isomorphous replacement with three heavy-atom derivatives. Least-squares refinement of the model reduced the crystallographic R factor to 18.1% for all measured X-ray data from 30.0 to 2.2 A. The overall fold of the molecule may be described as a seven-stranded antiparallel beta-barrel flanked on the bottom by two additional beta-strands and on the top by an alpha-helix. Quite surprisingly, the three-dimensional structure of this beta-barrel is not similar to telokin or to any other known protein.

Molecular structure of a proteolytic fragment of TLP20.,Holden HM, Wesenberg G, Raynes DA, Hartshorne DJ, Guerriero V Jr, Rayment I Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1153-60. PMID:15299576<ref>PMID:15299576</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 1tul" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Acmnpv]]

[[Category: Holden, H M]]

[[Category: Rayment, I]]

[[Category: Telokin-like protein]]