1al1: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1al1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AL1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AL1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1al1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AL1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AL1 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1al1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1al1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1al1 RCSB], [http://www.ebi.ac.uk/pdbsum/1al1 PDBsum]</span></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=1al1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1al1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1al1 RCSB], [http://www.ebi.ac.uk/pdbsum/1al1 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 19: | Line 19: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Anderson, D H | [[Category: Anderson, D H]] | ||
[[Category: Degrado, W F | [[Category: Degrado, W F]] | ||
[[Category: Eisenberg, D | [[Category: Eisenberg, D]] | ||
[[Category: Hill, C P | [[Category: Hill, C P]] | ||
[[Category: Wesson, L | [[Category: Wesson, L]] | ||
[[Category: Synthetic protein model]] | [[Category: Synthetic protein model]] | ||
Revision as of 13:56, 22 December 2014
CRYSTAL STRUCTURE OF ALPHA1: IMPLICATIONS FOR PROTEIN DESIGNCRYSTAL STRUCTURE OF ALPHA1: IMPLICATIONS FOR PROTEIN DESIGN
Structural highlights
Publication Abstract from PubMedX-ray diffraction shows the structure of a synthetic protein model, formed from noncovalent self-association of a 12-residue peptide and of sulfate ions at low pH. This peptide is a fragment of a 16-residue polypeptide that was designed to form an amphiphilic alpha helix with a ridge of Leu residues along one helical face. By interdigitation of the leucines of four such helices, the design called for self-association into a four-alpha-helical bundle. The crystal structure (2.7 angstrom resolution; R factor = 0.215) reveals a structure more complex than the design, with both a tetramer and a hexamer. The alpha-helical tetramer with leucine interior has more oblique crossing angles than most four-alpha-helical bundles; the hexamer has a globular hydrophobic core of 12 leucine residues and three associated sulfate ions. Computational analysis suggests that the hexameric association is tighter than the tetrameric one. The consistency of the structure with the design is discussed, as well as the divergence. Crystal structure of alpha 1: implications for protein design.,Hill CP, Anderson DH, Wesson L, DeGrado WF, Eisenberg D Science. 1990 Aug 3;249(4968):543-6. PMID:2382133[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
| ||||||||||||||||||