1dqc: Difference between revisions
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==SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTION== | ==SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTION== | ||
<StructureSection load='1dqc' size='340' side='right'caption='[[1dqc | <StructureSection load='1dqc' size='340' side='right'caption='[[1dqc]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dqc]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1dqc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tachypleus_tridentatus Tachypleus tridentatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DQC FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 25 models</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqc OCA], [https://pdbe.org/1dqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dqc RCSB], [https://www.ebi.ac.uk/pdbsum/1dqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dqc ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/P91818_TACTR P91818_TACTR] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dq/1dqc_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dq/1dqc_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 26: | Line 29: | ||
</div> | </div> | ||
<div class="pdbe-citations 1dqc" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1dqc" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 35: | Line 35: | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Tachypleus tridentatus]] | [[Category: Tachypleus tridentatus]] | ||
[[Category: Kawabata | [[Category: Kawabata S]] | ||
[[Category: Kawano | [[Category: Kawano K]] | ||
[[Category: Miura | [[Category: Miura K]] | ||
[[Category: Suetake | [[Category: Suetake T]] | ||
[[Category: Tsuda | [[Category: Tsuda S]] | ||
Latest revision as of 11:23, 6 November 2024
SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTIONSOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTION
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTachycitin, a 73-residue polypeptide having antimicrobial activity is present in the hemocyte of horseshoe crab (Tachypleus tridentatus). The first three-dimensional structure of invertebrate chitin-binding protein was determined for tachycitin using two-dimensional nuclear magnetic resonance spectroscopy. The measurements indicate that the structure of tachycitin is largely divided into N- and C-terminal domains; the former comprises a three-stranded beta-sheet and the latter a two-stranded beta-sheet following a short helical turn. The latter structural motif shares a significant tertiary structural similarity with the chitin-binding domain of plant chitin-binding protein. This result is thought to provide faithful experimental evidence to the recent hypothesis that chitin-binding proteins of invertebrates and plants are correlated by a convergent evolution process. Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif.,Suetake T, Tsuda S, Kawabata S, Miura K, Iwanaga S, Hikichi K, Nitta K, Kawano K J Biol Chem. 2000 Jun 16;275(24):17929-32. PMID:10770921[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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