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[[ | ==SOLUTION STRUCTURE OF A DE NOVO DESIGNED SINGLE CHAIN THREE-HELIX BUNDLE (A3D)== | ||
<StructureSection load='2a3d' size='340' side='right' caption='[[2a3d]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2a3d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. The October 2005 RCSB PDB [http://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 [http://dx.doi.org/10.2210/rcsb_pdb/mom_2005_10 10.2210/rcsb_pdb/mom_2005_10]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A3D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A3D FirstGlance]. <br> | |||
</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=2a3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a3d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2a3d RCSB], [http://www.ebi.ac.uk/pdbsum/2a3d PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Although de novo protein design is an important endeavor with implications for understanding protein folding, until now, structures have been determined for only a few 25- to 30-residue designed miniproteins. Here, the NMR solution structure of a complex 73-residue three-helix bundle protein, alpha3D, is reported. The structure of alpha3D was not based on any natural protein, and yet it shows thermodynamic and spectroscopic properties typical of native proteins. A variety of features contribute to its unique structure, including electrostatics, the packing of a diverse set of hydrophobic side chains, and a loop that incorporates common capping motifs. Thus, it is now possible to design a complex protein with a well defined and predictable three-dimensional structure. | |||
Solution structure and dynamics of a de novo designed three-helix bundle protein.,Walsh ST, Cheng H, Bryson JW, Roder H, DeGrado WF Proc Natl Acad Sci U S A. 1999 May 11;96(10):5486-91. PMID:10318910<ref>PMID:10318910</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Designer Proteins]] | [[Category: Designer Proteins]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
Revision as of 11:29, 8 October 2014
SOLUTION STRUCTURE OF A DE NOVO DESIGNED SINGLE CHAIN THREE-HELIX BUNDLE (A3D)SOLUTION STRUCTURE OF A DE NOVO DESIGNED SINGLE CHAIN THREE-HELIX BUNDLE (A3D)
Structural highlights
Publication Abstract from PubMedAlthough de novo protein design is an important endeavor with implications for understanding protein folding, until now, structures have been determined for only a few 25- to 30-residue designed miniproteins. Here, the NMR solution structure of a complex 73-residue three-helix bundle protein, alpha3D, is reported. The structure of alpha3D was not based on any natural protein, and yet it shows thermodynamic and spectroscopic properties typical of native proteins. A variety of features contribute to its unique structure, including electrostatics, the packing of a diverse set of hydrophobic side chains, and a loop that incorporates common capping motifs. Thus, it is now possible to design a complex protein with a well defined and predictable three-dimensional structure. Solution structure and dynamics of a de novo designed three-helix bundle protein.,Walsh ST, Cheng H, Bryson JW, Roder H, DeGrado WF Proc Natl Acad Sci U S A. 1999 May 11;96(10):5486-91. PMID:10318910[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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