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J. Biol. Chem., Vol. 277, Issue 6, 4223-4231, February 8, 2002
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From the Type I collagen is the most abundant protein in
humans, and it helps to maintain the integrity of many tissues via its
interactions with cell surfaces, other extracellular matrix molecules,
and growth and differentiation factors. Nearly 50 molecules have been found to interact with type I collagen, and for about half of them,
binding sites on this collagen have been elucidated. In addition, over
300 mutations in type I collagen associated with human connective
tissue disorders have been described. However, the spatial
relationships between the known ligand-binding sites and mutation
positions have not been examined. To this end, here we have created a
map of type I collagen that includes all of its ligand-binding sites
and mutations. The map reveals the existence of several hot spots for
ligand interactions on type I collagen and that most of the binding
sites locate to its C-terminal half. Moreover, on the collagen fibril
some potentially relevant relationships between binding sites were
observed including the following: fibronectin- and certain
integrin-binding regions are near neighbors, which may mechanistically
relate to fibronectin-dependent cell-collagen attachment;
proteoglycan binding may potentially impact upon collagen fibrillogenesis, cell-collagen attachment, and collagen glycation seen
in diabetes and aging; and mutations associated with osteogenesis imperfecta and other disorders show apparently nonrandom distribution patterns within both the monomer and fibril, implying that mutation positions correlate with disease phenotype. These and other
observations presented here may provide novel insights into evaluating
type I collagen functions and the relationships between its binding partners and mutations.
Mapping the Ligand-binding Sites and Disease-associated
Mutations on the Most Abundant Protein in the Human, Type I
Collagen*
,
, and§**
Department of Medicine and the Cardeza
Foundation for Hematologic Research and the § Department of
Pathology, Anatomy and Cell Biology, Thomas Jefferson University,
Philadelphia, Pennsylvania 19107, the ¶ Center of Gene Therapy and
Department of Medicine, Tulane University Health Sciences Center, New
Orleans, Louisiana 70112, and the Collagen Research Unit,
Biocenter and Department of Medical Biochemistry, University of
Oulu, 90220 Oulu, Finland
*
This work was supported by National Institutes of Health
Grant HL-53590 and American Heart Association Grant 9910067U (to J. S. A.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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