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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1993-10-4
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pubmed:databankReference |
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pubmed:abstractText |
Marfan syndrome results from mutations in an extracellular matrix glycoprotein, fibrillin. Previous studies have characterized approximately 6.9-kb of the estimated 10-kb fibrillin transcript. We have now completed the primary structure of fibrillin, elucidated the exon/intron organization of the gene and derived a physical map of the genetic locus. Pre-fibrillin consists of 2,871 amino acids which, excluding the signal peptide, are arranged into five structurally distinct regions. The largest of these regions comprises about 75% of the entire protein and consists of numerous repeated cysteine-rich sequences homologous to the peptide motifs of the epidermal growth factor (EGF) and transforming growth factor-beta binding protein (TGF-bp). Forty-three of the forty-six EGF-like repeats contain a calcium binding consensus sequence (EGF-CB) conceivably mediating protein-protein interactions. Fibrillin exhibits a few additional cysteine-rich modules that are apparently unique to this macromolecule and may represent evolutionary variants of the EGF-CB and TGF-bp motifs. Almost all of the cysteine-rich repeats are encoded by single exons; consequently, the fibrillin gene is relatively large (approximately 110-kb) and highly fragmented (65 exons). This study provides the first comprehensive analysis of the fibrillin gene and relevant information for the full characterization of Marfan syndrome mutations.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0964-6906
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
961-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8364578-Amino Acid Sequence,
pubmed-meshheading:8364578-Base Sequence,
pubmed-meshheading:8364578-Carrier Proteins,
pubmed-meshheading:8364578-Chromosome Mapping,
pubmed-meshheading:8364578-Chromosomes, Fungal,
pubmed-meshheading:8364578-Cloning, Molecular,
pubmed-meshheading:8364578-Cysteine,
pubmed-meshheading:8364578-DNA,
pubmed-meshheading:8364578-Epidermal Growth Factor,
pubmed-meshheading:8364578-Exons,
pubmed-meshheading:8364578-Gene Library,
pubmed-meshheading:8364578-Genome, Human,
pubmed-meshheading:8364578-Humans,
pubmed-meshheading:8364578-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:8364578-Latent TGF-beta Binding Proteins,
pubmed-meshheading:8364578-Marfan Syndrome,
pubmed-meshheading:8364578-Microfilament Proteins,
pubmed-meshheading:8364578-Molecular Sequence Data,
pubmed-meshheading:8364578-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:8364578-Transforming Growth Factor beta
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pubmed:year |
1993
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pubmed:articleTitle |
Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndrome.
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pubmed:affiliation |
Brookdale Center for Molecular Biology, Mount Sinai School of Medicine, New York, NY 10029.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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