Domains of laminin
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Domains of laminin. / Engvall, E; Wewer, U M.
I: Journal of Cellular Biochemistry, Bind 61, Nr. 4, 15.06.1996, s. 493-501.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - Domains of laminin
AU - Engvall, E
AU - Wewer, U M
PY - 1996/6/15
Y1 - 1996/6/15
N2 - Extracellular matrix molecules are often very large and made up of several independent domains, frequently with autonomous activities. Laminin is no exception. A number of globular and rod-like domains can be identified in laminin and its isoforms by sequence analysis as well as by electron microscopy. Here we present the structure-function relations in laminins by examination of their individual domains. This approach to viewing laminin is based on recent results from several laboratories. First, some mutations in laminin genes that cause disease have affected single laminin domains, and some laminin isoforms lack particular domains. These mutants and isoforms are informative with regard to the activities of the mutated and missing domains. These mutants and isoforms are informative with regard to the activities of the mutated and missing domains. Second, laminin-like domains have now been found in a number of other proteins, and data on these proteins may be informative in terms of structure-function relationships in laminin. Finally, a large body of data has accumulated on the structure and activities of proteolytic fragments, recombinant fragments, and synthetic peptides from laminin. The proposed activities of these domains can now be confirmed and extended by in vivo experiments.
AB - Extracellular matrix molecules are often very large and made up of several independent domains, frequently with autonomous activities. Laminin is no exception. A number of globular and rod-like domains can be identified in laminin and its isoforms by sequence analysis as well as by electron microscopy. Here we present the structure-function relations in laminins by examination of their individual domains. This approach to viewing laminin is based on recent results from several laboratories. First, some mutations in laminin genes that cause disease have affected single laminin domains, and some laminin isoforms lack particular domains. These mutants and isoforms are informative with regard to the activities of the mutated and missing domains. These mutants and isoforms are informative with regard to the activities of the mutated and missing domains. Second, laminin-like domains have now been found in a number of other proteins, and data on these proteins may be informative in terms of structure-function relationships in laminin. Finally, a large body of data has accumulated on the structure and activities of proteolytic fragments, recombinant fragments, and synthetic peptides from laminin. The proposed activities of these domains can now be confirmed and extended by in vivo experiments.
KW - Animals
KW - Humans
KW - Laminin
KW - Polymers
KW - Protein Structure, Secondary
KW - Protein Structure, Tertiary
KW - Structure-Activity Relationship
U2 - 10.1002/(SICI)1097-4644(19960616)61:4<493::AID-JCB2>3.0.CO;2-J
DO - 10.1002/(SICI)1097-4644(19960616)61:4<493::AID-JCB2>3.0.CO;2-J
M3 - Journal article
C2 - 8806072
VL - 61
SP - 493
EP - 501
JO - Journal of cellular biochemistry. Supplement
JF - Journal of cellular biochemistry. Supplement
SN - 0733-1959
IS - 4
ER -
ID: 34326069