1r3a: Difference between revisions
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{{Theoretical_model}} | |||
==THEORETICAL MODEL OF HUMAN GALACTOSE-1-PHOSPHATE URIDYLYL TRANSFERASE (GALT)== | |||
<StructureSection load='1r3a' size='340' side='right'caption='[[1r3a]]' 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=1R3A 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=1r3a FirstGlance], [https://www.ebi.ac.uk/pdbsum/1r3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r3a ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We have created theoretical models of the three-dimensional dimeric structure of human galactose-1-phosphate uridylyltransferase as well as of homo- and heterodimers carrying the Q188R mutation by using comparative modeling procedures. These mutants are associated to the most frequent form of the genetic disease galactosemia. We have analyzed the impact of this mutation both on enzyme-substrate interactions as well as on interchain interactions in the heterodimers and in the homodimer. We suggest a molecular explanation for the altered function, caused by different enzyme-substrate interactions, and for the partial dominant negative effect of the mutant allele that is present in heterozygotes for this gene, related to a substantial loss of interchain hydrogen bonds. These results can be considered a starting point for a more extensive characterization at the molecular level of the other mutations linked to this genetic disease. | |||
Homology modeling studies on human galactose-1-phosphate uridylyltransferase and on its galactosemia-related mutant Q188R provide an explanation of molecular effects of the mutation on homo- and heterodimers.,Marabotti A, Facchiano AM J Med Chem. 2005 Feb 10;48(3):773-9. PMID:15689161<ref>PMID:15689161</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1r3a" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Facchiano, A M]] | |||
[[Category: Marabotti, A]] | |||
Latest revision as of 13:07, 15 September 2021
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THEORETICAL MODEL OF HUMAN GALACTOSE-1-PHOSPHATE URIDYLYL TRANSFERASE (GALT)THEORETICAL MODEL OF HUMAN GALACTOSE-1-PHOSPHATE URIDYLYL TRANSFERASE (GALT)
Structural highlights
Publication Abstract from PubMedWe have created theoretical models of the three-dimensional dimeric structure of human galactose-1-phosphate uridylyltransferase as well as of homo- and heterodimers carrying the Q188R mutation by using comparative modeling procedures. These mutants are associated to the most frequent form of the genetic disease galactosemia. We have analyzed the impact of this mutation both on enzyme-substrate interactions as well as on interchain interactions in the heterodimers and in the homodimer. We suggest a molecular explanation for the altered function, caused by different enzyme-substrate interactions, and for the partial dominant negative effect of the mutant allele that is present in heterozygotes for this gene, related to a substantial loss of interchain hydrogen bonds. These results can be considered a starting point for a more extensive characterization at the molecular level of the other mutations linked to this genetic disease. Homology modeling studies on human galactose-1-phosphate uridylyltransferase and on its galactosemia-related mutant Q188R provide an explanation of molecular effects of the mutation on homo- and heterodimers.,Marabotti A, Facchiano AM J Med Chem. 2005 Feb 10;48(3):773-9. PMID:15689161[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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