Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC51117Laminin N-terminal (LN) domain profile
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC51117
Laminin is a large molecular weight glycoprotein present only in basement membranes in almost every animal tissue. Each laminin is a heterotrimer assembled from α, β and γ chain subunits, secreted and incorporated into cell-associated extracellular matrices [1].
Basement membrane assembly is a cooperative process in which laminins polymerize through their N-terminal domain (LN or domain VI) and anchor to the cell surface through their G domains (see <PDOC50025>). Netrins may also associate with this network through heterotypic LN domain interactions [2]. This leads to cell signaling through integrins and dystroglycan (and possibly other receptors) recruited to the adherent laminin. This LN domain dependent self-assembly is considered to be crucial for the integrity of basement membranes, as highlighted by genetic forms of muscular dystrophy containing the deletion of the LN module from the α 2 laminin chain [3].
The laminin N-terminal domain is found in all laminin and netrin subunits except laminin α 3A, α 4 and γ 2.
The profile we developed covers the whole laminin N-terminal domain.
Last update:April 2005 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Colognato H. Yurchenco P.D. |
| Title | Form and function: the laminin family of heterotrimers. | |
| Source | Dev. Dyn. 218:213-234(2000). | |
| PubMed ID | 10842354 | |
| DOI | 10.1002/(SICI)1097-0177(200006)218:2<213::AID-DVDY1>3.0.CO;2-R |
| 2 | Authors | Yurchenco P.D. Cheng Y.S. |
| Title | Self-assembly and calcium-binding sites in laminin. A three-arm interaction model. | |
| Source | J. Biol. Chem. 268:17286-17299(1993). | |
| PubMed ID | 8349613 |
| 3 | Authors | Xu H. Wu X.R. Wewer U.M. Engvall E. |
| Title | Murine muscular dystrophy caused by a mutation in the laminin alpha 2 (Lama2) gene. | |
| Source | Nat. Genet. 8:297-302(1994). | |
| PubMed ID | 7874173 | |
| DOI | 10.1038/ng1194-297 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.