1KMX
Heparin-binding Domain from Vascular Endothelial Growth Factor
Summary for 1KMX
| Entry DOI | 10.2210/pdb1kmx/pdb |
| Related | 1vgh 2vgh |
| NMR Information | BMRB: 5238 |
| Descriptor | vascular endothelial growth factor (1 entity in total) |
| Functional Keywords | heparin-binding, angiogenesis, growth factor, hormone-growth factor complex, hormone/growth factor |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P15692 |
| Total number of polymer chains | 1 |
| Total formula weight | 6496.48 |
| Authors | Stauffer, M.E.,Skelton, N.J.,Fairbrother, W.J. (deposition date: 2001-12-17, release date: 2002-07-24, Last modification date: 2024-10-09) |
| Primary citation | Stauffer, M.E.,Skelton, N.J.,Fairbrother, W.J. Refinement of the Solution Structure of the Heparin-binding Domain of Vascular Endothelial Growth Factor using Residual Dipolar Couplings J.BIOMOL.NMR, 23:57-61, 2002 Cited by PubMed Abstract: Previous NMR structural studies of the heparin-binding domain of vascular endothelial growth factor (VEGF165) revealed a novel fold comprising two subdomains, each containing two disulfide bridges and a short two-stranded antiparallel beta-sheet. The mutual orientation of the two subdomains was poorly defined by the NMR data. Heteronuclear relaxation data suggested that this disorder resulted from a relative lack of experimental restraints due to the limited size of the interface, rather than inherent high-frequency flexibility. Refinement of the structure using 1H(N-15N residual dipolar coupling restraints results in significantly improved definition of the relative subdomain orientations. PubMed: 12061718DOI: 10.1023/A:1015346504499 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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