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2esy

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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'''
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===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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16478467 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16478467}}
==About this Structure==
==About this Structure==
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ESY OCA].
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Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ESY OCA].
==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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:05:02 2008''
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''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

Image:2esy.png

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

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