From Proteopedia
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| | {{STRUCTURE_2esy| PDB=2esy | SCENE= }} | | {{STRUCTURE_2esy| PDB=2esy | SCENE= }} |
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| - | '''Structure and influence on stability and activity of the N-terminal propetide part of lung surfactant protein C'''
| + | ===Structure and influence on stability and activity of the N-terminal propetide part of lung surfactant protein C=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16478467}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16478467 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16478467}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ESY OCA]. | + | Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ESY OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Thyberg, J.]] | | [[Category: Thyberg, J.]] |
| | [[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 Sun May 4 03:05:02 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:24:36 2008'' |
Revision as of 18:24, 28 July 2008
Template:STRUCTURE 2esy
Structure and influence on stability and activity of the N-terminal propetide part of lung surfactant protein C
Template:ABSTRACT PUBMED 16478467
About this Structure
Full experimental 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 Mon Jul 28 21:24:36 2008
