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Statements

Subject Item
n2:RIV%2F61388963%3A_____%2F11%3A00389581%21RIV13-AV0-61388963
rdf:type
skos:Concept n18:Vysledek
dcterms:description
Aim To analyze the genesis of hypertrophic cardiomyopathy on a large cohort of patients from molecular genetics point of view and perform the functional analysis of the 3D molecular model of defective myosin-7 protein in silico. Methods The study enrolled 153 patients with diagnosed hypertrophic cardiomyopathy from different parts of the Czech Republic. DNA samples were analyzed for mutations in exons 21 and 22 of the MYH7 gene, which have been associated with high mutation clustering. The 3D model of human myosin-7 was built using the x-ray structure of nucleotide-free scallop myosin S1 as the structural template. We performed de novo structure prediction of mutant and wild type peptides spanning the 769-788 amino acids region of the myosin-7 protein. Results The Arg(870)His and Asp(778)Val amino acid alterations were found in 2 unrelated patients with a severe form of hypertrophic cardiomyopathy. The Asp(778)Val variation was chosen for subsequent 3D molecular modeling in silico. The mutation of the Asp by Val not only changes the character of the interaction pattern with other amino acids or ions but Val, being a small hydrophobic amino acid, can also completely change the stability of the region. Conclusion Mutation location in the MYH7 gene and changes in amino acid composition may have a crucial negative impact on the outcome of the disease in patients with hypertrophic cardiomyopathy. In addition, a mutation that changes the charge of the amino acid is more likely to affect protein function than a conservative mutation. Aim To analyze the genesis of hypertrophic cardiomyopathy on a large cohort of patients from molecular genetics point of view and perform the functional analysis of the 3D molecular model of defective myosin-7 protein in silico. Methods The study enrolled 153 patients with diagnosed hypertrophic cardiomyopathy from different parts of the Czech Republic. DNA samples were analyzed for mutations in exons 21 and 22 of the MYH7 gene, which have been associated with high mutation clustering. The 3D model of human myosin-7 was built using the x-ray structure of nucleotide-free scallop myosin S1 as the structural template. We performed de novo structure prediction of mutant and wild type peptides spanning the 769-788 amino acids region of the myosin-7 protein. Results The Arg(870)His and Asp(778)Val amino acid alterations were found in 2 unrelated patients with a severe form of hypertrophic cardiomyopathy. The Asp(778)Val variation was chosen for subsequent 3D molecular modeling in silico. The mutation of the Asp by Val not only changes the character of the interaction pattern with other amino acids or ions but Val, being a small hydrophobic amino acid, can also completely change the stability of the region. Conclusion Mutation location in the MYH7 gene and changes in amino acid composition may have a crucial negative impact on the outcome of the disease in patients with hypertrophic cardiomyopathy. In addition, a mutation that changes the charge of the amino acid is more likely to affect protein function than a conservative mutation.
dcterms:title
Hypertrophic cardiomyopathy: from mutation to functional analysis of defective protein Hypertrophic cardiomyopathy: from mutation to functional analysis of defective protein
skos:prefLabel
Hypertrophic cardiomyopathy: from mutation to functional analysis of defective protein Hypertrophic cardiomyopathy: from mutation to functional analysis of defective protein
skos:notation
RIV/61388963:_____/11:00389581!RIV13-AV0-61388963
n18:predkladatel
n19:ico%3A61388963
n3:aktivita
n12:S n12:P n12:V n12:Z
n3:aktivity
P(LN00B107), S, V, Z(AV0Z40550506)
n3:cisloPeriodika
3
n3:dodaniDat
n9:2013
n3:domaciTvurceVysledku
n20:7358946
n3:druhVysledku
n14:J
n3:duvernostUdaju
n16:S
n3:entitaPredkladatele
n10:predkladatel
n3:idSjednocenehoVysledku
203223
n3:idVysledku
RIV/61388963:_____/11:00389581
n3:jazykVysledku
n5:eng
n3:klicovaSlova
myosin heavy chain; homology modeling; molecular simulation; inherited cardiomyopathies
n3:klicoveSlovo
n8:molecular%20simulation n8:myosin%20heavy%20chain n8:inherited%20cardiomyopathies n8:homology%20modeling
n3:kodStatuVydavatele
HR - Chorvatská republika
n3:kontrolniKodProRIV
[AFB1E5E27CEE]
n3:nazevZdroje
Croatian Medical Journal
n3:obor
n6:CE
n3:pocetDomacichTvurcuVysledku
1
n3:pocetTvurcuVysledku
4
n3:projekt
n11:LN00B107
n3:rokUplatneniVysledku
n9:2011
n3:svazekPeriodika
52
n3:tvurceVysledku
Brdička, R. Škvor, J. Čapek, P. Vondrášek, Jiří
n3:wos
000292873600016
n3:zamer
n17:AV0Z40550506
s:issn
0353-9504
s:numberOfPages
8
n13:doi
10.3325/cmj.2011.52.384