1egb: Difference between revisions
New page: '''Theoretical Model''' The entry 1EGB is a Theoretical Model titled 'THEORETICAL MODEL OF THE BINDING DOMAIN OF A CELLOBIOHYDROLASE FROM CORIOLUS VERSICOLOR'. [[Category:Theoretical Mod... |
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{{Theoretical_model}} | |||
==THEORETICAL MODEL OF THE BINDING DOMAIN OF A CELLOBIOHYDROLASE FROM CORIOLUS VERSICOLOR== | |||
<StructureSection load='1egb' size='340' side='right'caption='[[1egb]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGB FirstGlance]. <br> | |||
</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=1egb FirstGlance], [https://www.ebi.ac.uk/pdbsum/1egb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egb ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Molecular cloning and cDNA sequencing analysis were used to elucidate the primary structure of a cellulase-like structure from the white-rot fungus Coriolus versicolor. The cDNA of interest was isolated from a cDNA library obtained from C. versicolor mycelia grown on cellulase inducer medium. A pattern search showed that this cellulase belongs to the glycosyl hydrolases family 6. From the deduced amino acid sequence, models of the binding and catalytic domains were built by homology modelling. The constructed models present a typical cellulose-binding domain at the N-terminal region, a rich Pro, Ser, Thr linker peptide, and a catalytic domain at the C-terminus region. | |||
Primary structure deduction and molecular modelling from a cDNA of a cellobiohydrolase-like protein from the white-rot fungus Coriolus versicolor.,Novo C, Simoes F, Mendonca D, Matos J, Clemente A Int J Biol Macromol. 2001 Apr 12;28(4):285-92. PMID:11311718<ref>PMID:11311718</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1egb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Clemente, A]] | |||
[[Category: Matos, J]] | |||
[[Category: Mendonca, D]] | |||
[[Category: Novo, C]] | |||
[[Category: Simoes, F]] | |||
Latest revision as of 14:08, 28 July 2021
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THEORETICAL MODEL OF THE BINDING DOMAIN OF A CELLOBIOHYDROLASE FROM CORIOLUS VERSICOLORTHEORETICAL MODEL OF THE BINDING DOMAIN OF A CELLOBIOHYDROLASE FROM CORIOLUS VERSICOLOR
Structural highlights
Publication Abstract from PubMedMolecular cloning and cDNA sequencing analysis were used to elucidate the primary structure of a cellulase-like structure from the white-rot fungus Coriolus versicolor. The cDNA of interest was isolated from a cDNA library obtained from C. versicolor mycelia grown on cellulase inducer medium. A pattern search showed that this cellulase belongs to the glycosyl hydrolases family 6. From the deduced amino acid sequence, models of the binding and catalytic domains were built by homology modelling. The constructed models present a typical cellulose-binding domain at the N-terminal region, a rich Pro, Ser, Thr linker peptide, and a catalytic domain at the C-terminus region. Primary structure deduction and molecular modelling from a cDNA of a cellobiohydrolase-like protein from the white-rot fungus Coriolus versicolor.,Novo C, Simoes F, Mendonca D, Matos J, Clemente A Int J Biol Macromol. 2001 Apr 12;28(4):285-92. PMID:11311718[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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