1M7L
Solution Structure of the Coiled-Coil Trimerization Domain from Lung Surfactant Protein D
Summary for 1M7L
| Entry DOI | 10.2210/pdb1m7l/pdb |
| Descriptor | Pulmonary surfactant-associated protein D (1 entity in total) |
| Functional Keywords | coiled coil, lung surfactant protein, trimer, ambiguous distance restraints, nmr-spectroscopy, sugar binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted, extracellular space, extracellular matrix: P35247 |
| Total number of polymer chains | 3 |
| Total formula weight | 13109.79 |
| Authors | Kovacs, H.,O'Donoghue, S.I.,Hoppe, H.-J.,Comfort, D.,Reid, K.B.M.,Campbell, I.D.,Nilges, M. (deposition date: 2002-07-22, release date: 2002-11-27, Last modification date: 2024-05-29) |
| Primary citation | Kovacs, H.,O'Donoghue, S.I.,Hoppe, H.-J.,Comfort, D.,Reid, K.B.M.,Campbell, I.D.,Nilges, M. Solution structure of the coiled-coil trimerization domain from lung surfactant protein D J.BIOMOL.NMR, 24:89-102, 2002 Cited by PubMed Abstract: Surfactant protein D (SP-D) is one of four known protein components of the pulmonary surfactant lining the lung alveoli. It is involved in immune and allergic responses. SP-D occurs as a tetramer of trimers. Trimerization is thought to be initiated by a coiled coil domain. We have determined the solution structure of a 64-residue peptide encompassing the coiled coil domain of human SP-D. As predicted, the domain forms a triple-helical parallel coiled coil. As with all symmetric oligomers, the structure calculation was complicated by the symmetry degeneracy in the NMR spectra. We used the symmetry-ADR (ambiguous distance restraint) structure calculation method to solve the structure. The results demonstrate that the leucine zipper region of SP-D is an autonomously folded domain. The structure is very similar to the independently determined X-ray crystal structure, differing mainly at a single residue, Tyr248. This residue is completely symmetric in the solution structure, and markedly asymmetric in the crystalline phase. This difference may be functionally important, as it affects the orientation of the antigenic surface presented by SP-D. PubMed: 12495025DOI: 10.1023/A:1020980006628 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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