rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
3
|
pubmed:dateCreated |
2002-6-7
|
pubmed:abstractText |
Conformational features of the C-terminal carboxyamidated pentadecapeptide of CCK (S(19)HRISDRD[SO(4)]-YMGWMDF(33)-NH(2)) were determined by NMR spectroscopy in a zwitterionic membrane-mimetic solvent system, composed of DPC micelles. The C-terminal octapeptide consisted of a well-defined pseudohelix that was nearly identical to the structure previously reported for nonsulfated CCK-8 in the same solvent system. N-terminal amino acids of CCK-15 were highly disordered, with no clear conformational preference. Extensive NOE-restrained molecular dynamics simulations of the CCK-15/CCK(1)-R complex suggested that almost all the experimentally determined intermolecular contact points provided by NMR, site-directed mutagenesis, and photoaffinity labeling could be simultaneously satisfied, when the N-terminus of the ligand is placed in close spatial proximity to the N-terminus of the receptor.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0006-291X
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pubmed:author |
|
pubmed:copyrightInfo |
(c) 2002 Elsevier Science (USA).
|
pubmed:issnType |
Print
|
pubmed:day |
10
|
pubmed:volume |
293
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1053-9
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:12051766-Amino Acid Sequence,
pubmed-meshheading:12051766-Animals,
pubmed-meshheading:12051766-Cholecystokinin,
pubmed-meshheading:12051766-Computer Simulation,
pubmed-meshheading:12051766-Micelles,
pubmed-meshheading:12051766-Models, Molecular,
pubmed-meshheading:12051766-Molecular Sequence Data,
pubmed-meshheading:12051766-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:12051766-Peptide Fragments,
pubmed-meshheading:12051766-Phosphorylcholine,
pubmed-meshheading:12051766-Protein Conformation,
pubmed-meshheading:12051766-Receptor, Cholecystokinin A,
pubmed-meshheading:12051766-Receptors, Cholecystokinin
|
pubmed:year |
2002
|
pubmed:articleTitle |
Conformational and molecular modeling studies of sulfated cholecystokinin-15.
|
pubmed:affiliation |
Department of Chemistry, Division of Biology & Medicine, Brown University, Providence, RI 02912, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|