1DYK
Laminin alpha 2 chain LG4-5 domain pair
Summary for 1DYK
| Entry DOI | 10.2210/pdb1dyk/pdb |
| Related | 1QU0 |
| Descriptor | LAMININ ALPHA 2 CHAIN, CALCIUM ION (3 entities in total) |
| Functional Keywords | metal binding protein, laminin |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) |
| Total number of polymer chains | 1 |
| Total formula weight | 42823.73 |
| Authors | Tisi, D.,Talts, J.F.,Timple, R.,Hohenester, E. (deposition date: 2000-02-01, release date: 2001-02-04, Last modification date: 2024-10-09) |
| Primary citation | Tisi, D.,Talts, J.F.,Timpl, R.,Hohenester, E. Structure of the C-Terminal Laminin G-Like Domain Pair of the Laminin Alpha 2 Chain Harbouring Binding Sites for Alpha-Dystroglycan and Heparin Embo J., 19:1432-, 2000 Cited by PubMed Abstract: The laminins are large heterotrimeric glycoproteins with fundamental roles in basement membrane architecture and function. The C-terminus of the laminin alpha chain contains a tandem of five laminin G-like (LG) domains. We report the 2.0 A crystal structure of the laminin alpha2 LG4-LG5 domain pair, which harbours binding sites for heparin and the cell surface receptor alpha-dystroglycan, and is 41% identical to the laminin alpha1 E3 fragment. LG4 and LG5 are arranged in a V-shaped fashion related by a 110 degrees rotation about an axis passing near the domain termini. An extended N-terminal segment is disulfide bonded to LG5 and stabilizes the domain pair. Two calcium ions, one each in LG4 and LG5, are located 65 A apart at the tips of the domains opposite the polypeptide termini. An extensive basic surface region between the calcium sites is proposed to bind alpha-dystroglycan and heparin. The LG4-LG5 structure was used to construct a model of the laminin LG1-LG5 tandem and interpret missense mutations underlying protein S deficiency. PubMed: 10747011DOI: 10.1093/EMBOJ/19.7.1432 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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