1HJ7
NMR study of a pair of LDL receptor Ca2+ binding epidermal growth factor-like domains, 20 structures
Summary for 1HJ7
| Entry DOI | 10.2210/pdb1hj7/pdb |
| Related | 1AJJ 1D2J 1EMO 1F5Y 1F8Z 1LDL 1LDR 1LRX |
| Descriptor | LDL RECEPTOR, CALCIUM ION (2 entities in total) |
| Functional Keywords | cell-surface receptor, calcium-binding, egf-like domain, module, apo-e, apo-b, ldl, vldl |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cell membrane ; Single-pass type I membrane protein : P01130 |
| Total number of polymer chains | 1 |
| Total formula weight | 8910.96 |
| Authors | Saha, S.,Handford, P.A.,Campbell, I.D.,Downing, A.K. (deposition date: 2001-01-09, release date: 2001-07-11, Last modification date: 2024-10-16) |
| Primary citation | Saha, S.,Boyd, J.,Werner, J.M.,Knott, V.,Handford, P.A.,Campbell, I.D.,Downing, A.K. Solution Structure of the Ldl Receptor Egf-Ab Pair: A Paradigm for the Assembly of Tandem Calcium Binding Egf Domains Structure, 9:451-, 2001 Cited by PubMed Abstract: From the observed structure and sequence of a pair of calcium binding (cb) epidermal growth factor-like (EGF) domains from human fibrillin-1, we proposed that many tandem cbEGF domains adopt a conserved relative conformation. The low-density lipoprotein receptor (LDLR), which is functionally unrelated to fibrillin-1, contains a single pair of EGF domains that was chosen for study in the validation of this hypothesis. The LDLR is the protein that is defective in familial hypercholesterolaemia, a common genetic disorder that predisposes individuals to cardiovascular complications and premature death. PubMed: 11435110DOI: 10.1016/S0969-2126(01)00606-2 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
