Publication Date:
1988-07-08
Description:
Gramicidin, a linear polypeptide composed of hydrophobic amino acids with alternating L- and D- configurations, forms transmembrane ion channels. The crystal structure of a gramicidin-cesium complex has been determined at 2.0 angstrom resolution. In this structure, gramicidin forms a 26 angstrom long tube comprised of two polypeptide chains arranged as antiparallel beta strands that are wrapped into a left-handed helical coil with 6.4 residues per turn. The polypeptide backbone forms the interior of the hydrophilic, solvent-filled pore and the side chains form a hydrophobic and relatively regular surface on the outside of the pore. This example of a crystal structure of a solvent-filled ion pore provides a basis for understanding the physical nature of ion translocation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallace, B A -- Ravikumar, K -- New York, N.Y. -- Science. 1988 Jul 8;241(4862):182-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Center for Biophysics, Rensselaer Polytechnic Institute, Troy, NY 12180.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2455344" target="_blank"〉PubMed〈/a〉
Keywords:
Binding Sites
;
Cesium
;
Computer Simulation
;
Crystallography
;
*Gramicidin
;
*Ion Channels
;
Ligands
;
Macromolecular Substances
;
*Membrane Proteins
;
Models, Molecular
;
Protein Conformation
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
Permalink