1spf: Difference between revisions
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<StructureSection load='1spf' size='340' side='right' caption='[[1spf]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1spf' size='340' side='right' caption='[[1spf]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1spf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1spf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SPF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SPF FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1spf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1spf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1spf RCSB], [http://www.ebi.ac.uk/pdbsum/1spf PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1spf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1spf OCA], [http://pdbe.org/1spf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1spf RCSB], [http://www.ebi.ac.uk/pdbsum/1spf PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1spf" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Pig]] | ||
[[Category: Curstedt, T]] | [[Category: Curstedt, T]] | ||
[[Category: Johansson, J]] | [[Category: Johansson, J]] | ||
[[Category: Szyperski, T]] | [[Category: Szyperski, T]] | ||
[[Category: Wuthrich, K]] | [[Category: Wuthrich, K]] | ||
Revision as of 03:24, 12 September 2015
THE NMR STRUCTURE OF THE PULMONARY SURFACTANT-ASSOCIATED POLYPEPTIDE SP-C IN AN APOLAR SOLVENT CONTAINS A VALYL-RICH ALPHA-HELIXTHE NMR STRUCTURE OF THE PULMONARY SURFACTANT-ASSOCIATED POLYPEPTIDE SP-C IN AN APOLAR SOLVENT CONTAINS A VALYL-RICH ALPHA-HELIX
Structural highlights
Function[PSPC_PIG] Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. Publication Abstract from PubMedThe nuclear magnetic resonance (NMR) structure of the pulmonary surfactant-associated lipoplypeptide C (SP-C) was determined in a mixed solvent of C2H3Cl/C2H3OH/ 1 M HCl 32:64:5 (v/v). Sequence-specific 1H NMR assignments and the collection of conformational constraints were achieved with two-dimensional 1H NMR, and the structure was calculated with the distance geometry program DIANA. The root mean square deviations for the well-defined polypeptide segment of residues 9-34 calculated for the 20 best energy-minimized DIANA conformers relative to their mean are 0.5 and 1.3 A for the polypeptide backbone atoms N, C alpha, and C', and for all heavy atoms, respectively. The 35-residue polypeptide chain of SP-C forms an alpha-helix between positions 9 and 34, which includes two segments of seven and four consecutive valyls that are separated by a single leucyl residue. The N-terminal hexapeptide segment, which includes two palmitoylcysteinyls, is flexibly disordered. The length of the alpha-helix is about 37 A, and the helical segment of residues 13-28, which contains exclusively aliphatic residues with branched side chains, is 23-A long and about 10 A in diameter. The alpha-helix is outstandingly regular, with virtually identical chi 1 angles for all valyl residues. The observation of a helical structure of SP-C was rather unexpected, considering that Val is generally underrepresented in alpha-helices, and it provides intriguing novel insights into the structural basis of SP-C functions as well as into general structural aspects of protein-lipid interactions in biological membranes. The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix.,Johansson J, Szyperski T, Curstedt T, Wuthrich K Biochemistry. 1994 May 17;33(19):6015-23. PMID:8180229[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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