1cos: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1cos]] is a 3 chain structure. The October 2005 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Designer Proteins'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2005_10 10.2210/rcsb_pdb/mom_2005_10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COS FirstGlance]. <br> | <table><tr><td colspan='2'>[[1cos]] is a 3 chain structure. The October 2005 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Designer Proteins'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2005_10 10.2210/rcsb_pdb/mom_2005_10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COS FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=1cos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cos OCA], [https://pdbe.org/1cos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cos RCSB], [https://www.ebi.ac.uk/pdbsum/1cos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cos ProSAT]</span></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=1cos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cos OCA], [https://pdbe.org/1cos PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cos RCSB], [https://www.ebi.ac.uk/pdbsum/1cos PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cos ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 11:22, 6 November 2024
CRYSTAL STRUCTURE OF A SYNTHETIC TRIPLE-STRANDED ALPHA-HELICAL BUNDLECRYSTAL STRUCTURE OF A SYNTHETIC TRIPLE-STRANDED ALPHA-HELICAL BUNDLE
Structural highlights
Publication Abstract from PubMedThe x-ray crystal structure of a peptide designed to form a double-stranded parallel coiled coil shows that it is actually a triple-stranded coiled coil formed by three alpha-helices. Unlike the designed parallel coiled coil, the helices run up-up-down. The structure is stabilized by a distinctive hydrophobic interface consisting of eight layers. As in the design, each alpha-helix in the coiled coil contributes one leucine side chain to each layer. The structure suggests that hydrophobic interactions are a dominant factor in the stabilization of coiled coils. The stoichiometry and geometry of coiled coils are primarily determined by side chain packing in the solvent-inaccessible interior, but electrostatic interactions also contribute. Crystal structure of a synthetic triple-stranded alpha-helical bundle.,Lovejoy B, Choe S, Cascio D, McRorie DK, DeGrado WF, Eisenberg D Science. 1993 Feb 26;259(5099):1288-93. PMID:8446897[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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