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laminin
EntityQ58345· pop 23· linked from 306 articles

thumb|Illustration of the laminin-111 complex depicting the domain organization. Laminins are a family of glycoproteins of the extracellular matrix of all animals. They are major constituents of the basement membrane, namely the basal lamina (the protein network foundation for most cells and organs). Laminins are vital to biological activity, influencing cell differentiation, migration, and adhesion.

Key facts

Protein family.Symbol
Laminin_N
Protein family.Name
Laminin N-terminal (Domain VI)
Protein family.Pfam
PF00055
Protein family.InterPro
IPR008211
Protein family.caption
the structure of the ligand-binding domain of neurexin 1beta: regulation of lns domain function by alternative splicing
Protein family.image
PDB 1c4r EBI.jpg
Protein family.Pfam_clan
CL0202
Protein family.PROSITE
PDOC00021
Protein family.SCOP
1klo
Protein family.SMART
LamNT

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Research

29,312 papers

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Wikidata facts

Image
Laminin111.png
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Commons category
Laminin
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via Wikidata · CC0

~15 min read

Article

17 sections
Contents
  • Types
  • Function
  • Role in neural development
  • Role in peripheral nerve repair
  • Pathology
  • Role in cancer
  • Use in cell culture
  • Laminin domains
  • Laminin I and Laminin II
  • Laminin B
  • Laminin EGF-like
  • Laminin G
  • Laminin N-terminal
  • Human proteins containing laminin domains
  • See also
  • References
  • External links

thumb|Illustration of the laminin-111 complex depicting the domain organization. Laminins are a family of glycoproteins of the extracellular matrix of all animals. They are major constituents of the basement membrane, namely the basal lamina (the protein network foundation for most cells and organs). Laminins are vital to biological activity, influencing cell differentiation, migration, and adhesion.

Laminins are heterotrimeric protein complexes with a high molecular mass (~400 to ~900 kDa) and possess three different chains (α, β, and γ) encoded by five, four, and three paralogous genes in humans, respectively. The laminin molecules are named according to their chain composition, e.g. laminin-511 contains α5, β1, and γ1 chains. Fourteen other chain combinations have been identified in vivo. The trimeric proteins intersect, composing a cruciform structure that is able to bind to other molecules of the extracellular matrix and cell membrane. The three short arms have an affinity for binding to other laminin molecules, conducing sheet formation. The long arm is capable of binding to cells and helps anchor organized tissue cells to the basement membrane.

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