1LM8
Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex
Summary for 1LM8
| Entry DOI | 10.2210/pdb1lm8/pdb |
| Descriptor | ELONGIN B, ELONGIN C, Von Hippel-Lindau disease tumor suppressor, ... (5 entities in total) |
| Functional Keywords | regulation, tumor suppressor, oxygen sensing, transcription |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus : Q15370 Q15369 Isoform 1: Cytoplasm. Isoform 3: Cytoplasm: P40337 Cytoplasm : Q16665 |
| Total number of polymer chains | 4 |
| Total formula weight | 44977.09 |
| Authors | Min, J.-H.,Yang, H.,Ivan, M.,Gertler, F.,Kaelin JR., W.G.,Pavletich, N.P. (deposition date: 2002-04-30, release date: 2002-06-12, Last modification date: 2023-08-16) |
| Primary citation | Min, J.H.,Yang, H.,Ivan, M.,Gertler, F.,Kaelin Jr., W.G.,Pavletich, N.P. Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling. Science, 296:1886-1889, 2002 Cited by PubMed Abstract: The ubiquitination of the hypoxia-inducible factor (HIF) by the von Hippel-Lindau tumor suppressor (pVHL) plays a central role in the cellular response to changes in oxygen availability. pVHL binds to HIF only when a conserved proline in HIF is hydroxylated, a modification that is oxygen-dependent. The 1.85 angstrom structure of a 20-residue HIF-1alpha peptide-pVHL-ElonginB-ElonginC complex shows that HIF-1alpha binds to pVHL in an extended beta strand-like conformation. The hydroxyproline inserts into a gap in the pVHL hydrophobic core, at a site that is a hotspot for tumorigenic mutations, with its 4-hydroxyl group recognized by buried serine and histidine residues. Although the beta sheet-like interactions contribute to the stability of the complex, the hydroxyproline contacts are central to the strict specificity characteristic of signaling. PubMed: 12004076DOI: 10.1126/science.1073440 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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