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Article

The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1.

The Journal of biological chemistry - 24 Mar 1995

Handford P, Downing A K, Rao Z, Hewett D R, Sykes B C, Kielty C M

Abstract excerpt

Human fibrillin-1 is a 350-kDa glycoprotein found in 10-nm connective tissue microfibrils. Mutations in the gene encoding this protein cause the Marfan syndrome, a disease characterized by cardiovascular, ocular, and skeletal abnormalities. Fibrillin-1 has a modular structure that includes 47 epidermal growth factor-like (EGF-like) domains, 43 of which contain a consensus sequence associated with calcium binding....

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Source

Identifiers

PMID: 7896820
DOI: 10.1074/jbc.270.12.6751

Genes

EGF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

The calcium binding properties and molecular organization of epidermal growth factor-like domains in human fibrillin-1.PMID 7896820Read ↗

Fibrillin domain folding and calcium binding: significance to Marfan syndrome.Semantic proximity Read ↗

Fibrillin-1, a calcium binding protein of extracellular matrix.Semantic proximity Read ↗

A Gly --> Ser change causes defective folding in vitro of calcium-binding epidermal growth factor-like domains from factor IX and fibrillin-1.Semantic proximity Read ↗

The extracellular matrix glycoprotein fibrillin-1 in health and diseaseSemantic proximity Read ↗

Genomic organization of the sequence coding for fibrillin, the defective gene product in Marfan syndromeSemantic proximity Read ↗

Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders.Semantic proximity Read ↗

The fibrillin-Marfan syndrome connection.Semantic proximity Read ↗

Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1.Semantic proximity Read ↗

Cellular and molecular studies of Marfan syndrome mutations identify co-operative protein folding in the cbEGF12-13 region of fibrillin-1.Semantic proximity Read ↗

Mutations in calcium-binding epidermal growth factor modules render fibrillin-1 susceptible to proteolysis. A potential disease-causing mechanism in Marfan syndrome.Semantic proximity Read ↗

A G1127S change in calcium-binding epidermal growth factor-like domain 13 of human fibrillin-1 causes short range conformational effects.Semantic proximity Read ↗

Fibrillin microfibril structure identifies long-range effects of inherited pathogenic mutations affecting a key regulatory TGFβ-binding siteSemantic proximity Read ↗

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