1M7L

Solution Structure of the Coiled-Coil Trimerization Domain from Lung Surfactant Protein D

1M7L の概要

• エントリーDOI: 10.2210/pdb1m7l/pdb
• 分子名称: Pulmonary surfactant-associated protein D (1 entity in total)
• 機能のキーワード: coiled coil, lung surfactant protein, trimer, ambiguous distance restraints, nmr-spectroscopy, sugar binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix: P35247
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 13109.79

構造登録者

Kovacs, H.,O'Donoghue, S.I.,Hoppe, H.-J.,Comfort, D.,Reid, K.B.M.,Campbell, I.D.,Nilges, M. (登録日: 2002-07-22, 公開日: 2002-11-27, 最終更新日: 2024-05-29)

主引用文献

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

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: 12495025
DOI: 10.1023/A:1020980006628

実験手法

SOLUTION NMR