Common structural motifs in proteins of the extracellular matrix

doi:10.1016/0955-0674(91)90050-9

Current Opinion in Cell Biology

Volume 3, Issue 5, October 1991, Pages 779-785

https://doi.org/10.1016/0955-0674(91)90050-9 Get rights and content

Abstract

Proteins of the extracellular matrix are composed of many structurally and often functionally different autonomous domains which frequently occur as modular units in several different extracellular matrix proteins, but also in proteins of different origin. Some domains serve related assembly functions in different proteins but for domains involved in cell attachment and other cellular activities only a few generalizations are possible.

References (45)

E.M. Hedgecock et al.
The unc-5, unc-6, and unc-40 Genes Guide Circumferential Migrations of Pioneer Axons and Mesodermal Cells on the Epidermis in C elegans
Neuron
(1990)
A. Lupas et al.
Predicting Coiled-Coils from Protein Sequences
Science
(1991)
J. Lawler et al.
Structural Organization of the Thrombospondin Molecule
Semin Thromb Hemostasis
(1987)
P. Bonaldo et al.
Structural and Functional Features of the α3 Chain Indicate a Bridging Role for Chicken Collagen VI in Connective Tissues
Biochemistry
(1990)
M.-L. Chu et al.
Mosaic Structure of Globular Domains 4n the Human Type VI Collagen Alpha 3 Chain: Similarity to von Willebrand Factor, Fibronectin, Actin, Salivary Proteins and Aprotinin Type Protease Inhibitors
EMBO J
(1990)
M. Paulsson et al.
Structure of Low Density Heparan Sulfate Proteoglycan Isolated from a Mouse Tumor Basement Membrane
J Mol Biol
(1987)
R.I. Hunter et al.
Evidence for a Specific Mechanism of Laminin Assembly
Eur J Biochem
(1990)
J. Engel et al.
Assembly of Laminin Isoforms by Triple and Double Stranded Coiled-Coil Structures
BioCHem Soc Transactions
(1991)
M. Aumailley et al.
Cell Attachment Properties of Collagen Type VI and Arg-Gly-Asp Dependent Binding to its Alpha 2 (VI) and Alpha 3 (VI) Chains
Exp Cell Res
(1989)
J. Engel
EGF-Like Domains in Extracellular Matrix Proteins: Localized Signals for Growth and Differentiation?
FEBS Lett
(1989)

E. Ruoslahti et al.

Proteoglycans as Modulators of Growth Factor Activity

Cell

(1991)

H. Kido et al.

Protease-Specificity of Kunitz Inhibitor Domain of Alzheimer's Disease Amyloid Protein Precursor

Biochem Biophys Res Commun

(1990)

K. Beck et al.

Structure and Function of Laminin: Anatomy of a Multidomain Glycoprotein

FASEB J

(1990)

J.R. Sanes et al.

Molecular Heterogeneity of Basal Laminae — Isoforms of Laminin and Collagen IV at the Neuromuscular Junction and Elsewhere

J Cell Biol

(1990)

G. Klein et al.

Differential Expression of Laminin-A and Laminin-B Chains During Development of Embryonic Mouse Organs

Development

(1990)

R.F. Doolittle

The Geneology of Some Recently Evolved Vertebrate Proteins

Trends Biochem Sci

(1985)

R.F. Doolittle et al.

Relationship of Human Protein Sequence to Those of Other Organisms

Cold Spring Harbor Symp Quant Biol

(1986)

C. Cohen et al.

α-Helical Coiled-Coils and Bundles: How to Design an α-Helical Protein

Proteins

(1990)

S. Suzuki et al.

Amino Acid Sequence of a Novel Integrin Beta 4 Subunit and Primary Expression of the mRNA in Epithelial Cells

EMBO J

(1990)

F. Hogervorst et al.

Cloning and Sequence Analysis of Beta-4 cDNA: an Integrin Subunit that Contains a Unique 118 kD Cytoplasmic Domain

EMBO J

(1990)

G.M. Benian et al.

Sequence of an Unusually Large Protein Implicated in Regulation of Myosin Activity 4n C. elegans

Nature

(1989)

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Citation Excerpt :
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View full text

Common structural motifs in proteins of the extracellular matrix

Abstract

Neuron

Science

Semin Thromb Hemostasis

Biochemistry

EMBO J

J Mol Biol

Eur J Biochem

BioCHem Soc Transactions

Exp Cell Res

FEBS Lett

Cell

Biochem Biophys Res Commun

Structure and Function of Laminin: Anatomy of a Multidomain Glycoprotein

FASEB J

Molecular Heterogeneity of Basal Laminae — Isoforms of Laminin and Collagen IV at the Neuromuscular Junction and Elsewhere

J Cell Biol

Differential Expression of Laminin-A and Laminin-B Chains During Development of Embryonic Mouse Organs

Development

The Geneology of Some Recently Evolved Vertebrate Proteins

Trends Biochem Sci

Relationship of Human Protein Sequence to Those of Other Organisms

Cold Spring Harbor Symp Quant Biol

α-Helical Coiled-Coils and Bundles: How to Design an α-Helical Protein

Proteins

Amino Acid Sequence of a Novel Integrin Beta 4 Subunit and Primary Expression of the mRNA in Epithelial Cells

EMBO J

Cloning and Sequence Analysis of Beta-4 cDNA: an Integrin Subunit that Contains a Unique 118 kD Cytoplasmic Domain

EMBO J

Sequence of an Unusually Large Protein Implicated in Regulation of Myosin Activity 4n C. elegans

Nature