1lbj: Difference between revisions
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==NMR solution structure of motilin in phospholipid bicellar solution== | |||
<StructureSection load='1lbj' size='340' side='right'caption='[[1lbj]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1lbj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LBJ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lbj OCA], [https://pdbe.org/1lbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lbj RCSB], [https://www.ebi.ac.uk/pdbsum/1lbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lbj ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MOTI_HUMAN MOTI_HUMAN] Plays an important role in the regulation of interdigestive gastrointestinal motility and indirectly causes rhythmic contraction of duodenal and colonic smooth muscle. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structure and dynamics of the gastrointestinal peptide hormone motilin, consisting of 22 amino acid residues, have been studied in the presence of isotropic q = 0.5 phospholipid bicelles. The NMR solution structure of the peptide in acidic bicelle solution was determined from 203 NOE-derived distance constraints and six backbone torsion angle constraints. Dynamic properties for the 13Calpha-1H vector in Leu10 were determined for motilin specifically labeled with 13C at this position by analysis of multiple-field relaxation data. The structure reveals an ordered alpha-helical conformation between Glu9 and Lys20. The N-terminus is also well structured with a turn resembling that of a classical beta-turn. The 13C dynamics clearly show that motilin tumbles slowly in solution, with a correlation time characteristic of a large object. It was also found that motilin has a large degree of local flexibility as compared with what has previously been reported in SDS micelles. The results show that motilin interacts with the bicelle, displaying motional properties of a peptide bound to a membrane. In comparison, motilin in neutral bicelles seems less structured and more flexible. This study shows that the small isotropic bicelles are well suited for use as membrane-mimetic for structural as well as dynamical investigations of membrane-bound peptides by high-resolution NMR. | |||
NMR solution structure and dynamics of motilin in isotropic phospholipid bicellar solution.,Andersson A, Maler L J Biomol NMR. 2002 Oct;24(2):103-12. PMID:12495026<ref>PMID:12495026</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1lbj" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Motilin|Motilin]] | *[[Motilin|Motilin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: A | [[Category: Large Structures]] | ||
[[Category: | [[Category: Andersson A]] | ||
[[Category: Maler L]] | |||
