2Y38
LAMININ ALPHA5 CHAIN N-TERMINAL FRAGMENT
Summary for 2Y38
| Entry DOI | 10.2210/pdb2y38/pdb |
| Descriptor | LAMININ SUBUNIT ALPHA-5, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | structural protein, cell adhesion, basement membrane |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) |
| Total number of polymer chains | 1 |
| Total formula weight | 45971.29 |
| Authors | Hussain, S.A.,Carafoli, F.,Hohenester, E. (deposition date: 2010-12-19, release date: 2011-02-23, Last modification date: 2024-11-20) |
| Primary citation | Hussain, S.A.,Carafoli, F.,Hohenester, E. Determinants of Laminin Polymerisation Revealed by the Crystal Structure of the Alpha5 Chain Amino-Terminal Region Embo Rep., 12:276-, 2011 Cited by PubMed Abstract: The polymerization of laminin into a cell-associated network--a key step in basement membrane assembly--is mediated by the laminin amino-terminal (LN) domains at the tips of the three short arms of the laminin αβγ-heterotrimer. The crystal structure of a laminin α5LN-LE1-2 fragment shows that the LN domain is a β-jelly roll with several elaborate insertions that is attached like a flower head to the stalk-like laminin-type epidermal growth factor-like tandem. A surface loop that is strictly conserved in the LN domains of all α-short arms is required for stable ternary association with the β- and γ-short arms in the laminin network. PubMed: 21311558DOI: 10.1038/EMBOR.2011.3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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