2OQP
Solution structure of human interleukin-21
Summary for 2OQP
| Entry DOI | 10.2210/pdb2oqp/pdb |
| Descriptor | Interleukin-21 (1 entity in total) |
| Functional Keywords | four helix bundle, cytokine, multiple conformers |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: Q9HBE4 |
| Total number of polymer chains | 1 |
| Total formula weight | 15622.89 |
| Authors | Bondensgaard, K.,Breinholt, J. (deposition date: 2007-02-01, release date: 2007-06-19, Last modification date: 2024-10-09) |
| Primary citation | Bondensgaard, K.,Breinholt, J.,Madsen, D.,Omkvist, D.H.,Kang, L.,Worsaae, A.,Becker, P.,Schiodt, C.B.,Hjorth, S.A. The existence of multiple conformers of interleukin-21 directs engineering of a superpotent analogue. J.Biol.Chem., 282:23326-23336, 2007 Cited by PubMed Abstract: The high resolution three-dimensional structure of human interleukin (hIL)-21 has been resolved by heteronuclear NMR spectroscopy. Overall, the hIL-21 structure is dominated by a well defined central four-helical bundle, arranged in an up-up-down-down topology, as observed for other cytokines. A segment of the hIL-21 molecule that includes the third helical segment, helix C, is observed to exist in two distinct and interchangeable states. In one conformer, the helix C segment is presented in a regular, alpha-helical conformation, whereas in the other conformer, this segment is largely disordered. A structure-based sequence alignment of hIL-21 with receptor complexes of the related cytokines, interleukin-2 and -4, implied that this particular segment is involved in receptor binding. An hIL-21 analog was designed to stabilize the region around helix C through the introduction of a segment grafted from hIL-4. This novel hIL-21 analog was demonstrated to exhibit a 10-fold increase in potency in a cellular assay. PubMed: 17565991DOI: 10.1074/jbc.M701313200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
