1ssz
From Proteopedia
(New page: 200px<br /> <applet load="1ssz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ssz" /> '''Conformational mapping of mini-b: an n-term...) |
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| - | [[Image:1ssz.gif|left|200px]]<br /> | + | [[Image:1ssz.gif|left|200px]]<br /><applet load="1ssz" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ssz" size=" | + | |
caption="1ssz" /> | caption="1ssz" /> | ||
'''Conformational mapping of mini-b: an n-terminal/c-terminal construct of surfactant protein b using 13c-enhanced fourier transform infrared (FTIR) spectroscopy'''<br /> | '''Conformational mapping of mini-b: an n-terminal/c-terminal construct of surfactant protein b using 13c-enhanced fourier transform infrared (FTIR) spectroscopy'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Surfactant protein B (SP-B) is essential for normal lung surfactant | + | Surfactant protein B (SP-B) is essential for normal lung surfactant function. Theoretical models predict that the disulfide cross-linked, N- and C-terminal domains of SP-B fold as charged amphipathic helices, and suggest that these adjacent helices participate in critical surfactant activities. This hypothesis is tested using a disulfide-linked construct (Mini-B) based on the primary sequences of the N- and C-terminal domains. Consistent with theoretical predictions of the full-length protein, both isotope-enhanced Fourier transform infrared (FTIR) spectroscopy and molecular modeling confirm the presence of charged amphipathic alpha-helices in Mini-B. Similar to that observed with native SP-B, Mini-B in model surfactant lipid mixtures exhibits marked in vitro activity, with spread films showing near-zero minimum surface tensions during cycling using captive bubble surfactometry. In vivo, Mini-B shows oxygenation and dynamic compliance that compare favorably with that of full-length SP-B. Mini-B variants (i.e. reduced disulfides or cationic residues replaced by uncharged residues) or Mini-B fragments (i.e. unlinked N- and C-terminal domains) produced greatly attenuated in vivo and in vitro surfactant properties. Hence, the combination of structure and charge for the amphipathic alpha-helical N- and C-terminal domains are key to SP-B function. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SSZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1SSZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SSZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacon, D.]] | [[Category: Bacon, D.]] | ||
[[Category: Braun, A.]] | [[Category: Braun, A.]] | ||
| - | [[Category: Gordon, L | + | [[Category: Gordon, L M.]] |
| - | [[Category: Hernandez-Juviel, J | + | [[Category: Hernandez-Juviel, J M.]] |
[[Category: Hong, T.]] | [[Category: Hong, T.]] | ||
| - | [[Category: Sherman, M | + | [[Category: Sherman, M A.]] |
| - | [[Category: Walther, F | + | [[Category: Walther, F J.]] |
| - | [[Category: Waring, A | + | [[Category: Waring, A J.]] |
| - | [[Category: Zasadzinski, J | + | [[Category: Zasadzinski, J A.]] |
[[Category: lung surfactant protein]] | [[Category: lung surfactant protein]] | ||
[[Category: saposin]] | [[Category: saposin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:54 2008'' |
Revision as of 13:04, 21 February 2008
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Conformational mapping of mini-b: an n-terminal/c-terminal construct of surfactant protein b using 13c-enhanced fourier transform infrared (FTIR) spectroscopy
Contents |
Overview
Surfactant protein B (SP-B) is essential for normal lung surfactant function. Theoretical models predict that the disulfide cross-linked, N- and C-terminal domains of SP-B fold as charged amphipathic helices, and suggest that these adjacent helices participate in critical surfactant activities. This hypothesis is tested using a disulfide-linked construct (Mini-B) based on the primary sequences of the N- and C-terminal domains. Consistent with theoretical predictions of the full-length protein, both isotope-enhanced Fourier transform infrared (FTIR) spectroscopy and molecular modeling confirm the presence of charged amphipathic alpha-helices in Mini-B. Similar to that observed with native SP-B, Mini-B in model surfactant lipid mixtures exhibits marked in vitro activity, with spread films showing near-zero minimum surface tensions during cycling using captive bubble surfactometry. In vivo, Mini-B shows oxygenation and dynamic compliance that compare favorably with that of full-length SP-B. Mini-B variants (i.e. reduced disulfides or cationic residues replaced by uncharged residues) or Mini-B fragments (i.e. unlinked N- and C-terminal domains) produced greatly attenuated in vivo and in vitro surfactant properties. Hence, the combination of structure and charge for the amphipathic alpha-helical N- and C-terminal domains are key to SP-B function.
Disease
Known disease associated with this structure: Surfactant metabolism dysfunction, pulmonary, 1 OMIM:[178640]
About this Structure
1SSZ is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
The role of charged amphipathic helices in the structure and function of surfactant protein B., Waring AJ, Walther FJ, Gordon LM, Hernandez-Juviel JM, Hong T, Sherman MA, Alonso C, Alig T, Braun A, Bacon D, Zasadzinski JA, J Pept Res. 2005 Dec;66(6):364-74. PMID:16316452
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