2esy
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2esy.gif|left|200px]] | + | [[Image:2esy.gif|left|200px]] |
| - | + | ||
| - | '''Structure and influence on stability and activity of the N-terminal propetide part of lung surfactant protein C''' | + | {{Structure |
| + | |PDB= 2esy |SIZE=350|CAPTION= <scene name='initialview01'>2esy</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure and influence on stability and activity of the N-terminal propetide part of lung surfactant protein C''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2ESY is a [ | + | 2ESY is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ESY OCA]. |
==Reference== | ==Reference== | ||
| - | Structure and influence on stability and activity of the N-terminal propeptide part of lung surfactant protein C., Li J, Liepinsh E, Almlen A, Thyberg J, Curstedt T, Jornvall H, Johansson J, FEBS J. 2006 Mar;273(5):926-35. PMID:[http:// | + | Structure and influence on stability and activity of the N-terminal propeptide part of lung surfactant protein C., Li J, Liepinsh E, Almlen A, Thyberg J, Curstedt T, Jornvall H, Johansson J, FEBS J. 2006 Mar;273(5):926-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16478467 16478467] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Almlen, A.]] | [[Category: Almlen, A.]] | ||
| Line 22: | Line 31: | ||
[[Category: n-terminal part of lung surfactant protein c]] | [[Category: n-terminal part of lung surfactant protein c]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:44:01 2008'' |
Revision as of 14:44, 20 March 2008
| |||||||
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure and influence on stability and activity of the N-terminal propetide part of lung surfactant protein C
Overview
Mature lung surfactant protein C (SP-C) corresponds to residues 24-58 of the 21 kDa proSP-C. A late processing intermediate, SP-Ci, corresponding to residues 12-58 of proSP-C, lacks the surface activity of SP-C, and the SP-Ci alpha-helical structure does not unfold in contrast to the metastable nature of the SP-C helix. The NMR structure of an analogue of SP-Ci, SP-Ci(1-31), with two palmitoylCys replaced by Phe and four Val replaced by Leu, in dodecylphosphocholine micelles and in ethanol shows that its alpha-helix vs. that of SP-C is extended N-terminally. The Arg-Phe part in SP-Ci that is cleaved to generate SP-C is localized in a turn structure, which is followed by a short segment in extended conformation. Circular dichroism spectroscopy of SP-Ci(1-31) in microsomal or surfactant lipids shows a mixture of helical and extended conformation at pH 6, and a shift to more unordered structure at pH 5. Replacement of the N-terminal hexapeptide segment SPPDYS (known to constitute a signal in intracellular targeting) of SP-Ci with AAAAAA results in a peptide that is mainly unstructured, independent of pH, in microsomal and surfactant lipids. Addition of a synthetic dodecapeptide, corresponding to the propeptide part of SP-Ci, to mature SP-C results in slower aggregation kinetics and altered amyloid fibril formation, and reduces the surface activity of phospholipid-bound SP-C. These data suggest that the propeptide part of SP-Ci prevents unfolding by locking the N-terminal part of the helix, and that acidic pH results in structural disordering of the region that is proteolytically cleaved to generate SP-C.
About this Structure
2ESY is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Structure and influence on stability and activity of the N-terminal propeptide part of lung surfactant protein C., Li J, Liepinsh E, Almlen A, Thyberg J, Curstedt T, Jornvall H, Johansson J, FEBS J. 2006 Mar;273(5):926-35. PMID:16478467
Page seeded by OCA on Thu Mar 20 16:44:01 2008
