1rh4: Difference between revisions

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[[Image:1rh4.gif|left|200px]]


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==RH4 DESIGNED RIGHT-HANDED COILED COIL TETRAMER==
The line below this paragraph, containing "STRUCTURE_1rh4", creates the "Structure Box" on the page.
<StructureSection load='1rh4' size='340' side='right'caption='[[1rh4]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1rh4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. 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=1RH4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RH4 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<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=IIL:ISO-ISOLEUCINE'>IIL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
{{STRUCTURE_1rh4| PDB=1rh4  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rh4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rh4 OCA], [https://pdbe.org/1rh4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rh4 RCSB], [https://www.ebi.ac.uk/pdbsum/1rh4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rh4 ProSAT]</span></td></tr>
 
</table>
'''RH4 DESIGNED RIGHT-HANDED COILED COIL TETRAMER'''
<div style="background-color:#fffaf0;">
 
== Publication Abstract from PubMed ==
 
==Overview==
Recent advances in computational techniques have allowed the design of precise side-chain packing in proteins with predetermined, naturally occurring backbone structures. Because these methods do not model protein main-chain flexibility, they lack the breadth to explore novel backbone conformations. Here the de novo design of a family of alpha-helical bundle proteins with a right-handed superhelical twist is described. In the design, the overall protein fold was specified by hydrophobic-polar residue patterning, whereas the bundle oligomerization state, detailed main-chain conformation, and interior side-chain rotamers were engineered by computational enumerations of packing in alternate backbone structures. Main-chain flexibility was incorporated through an algebraic parameterization of the backbone. The designed peptides form alpha-helical dimers, trimers, and tetramers in accord with the design goals. The crystal structure of the tetramer matches the designed structure in atomic detail.
Recent advances in computational techniques have allowed the design of precise side-chain packing in proteins with predetermined, naturally occurring backbone structures. Because these methods do not model protein main-chain flexibility, they lack the breadth to explore novel backbone conformations. Here the de novo design of a family of alpha-helical bundle proteins with a right-handed superhelical twist is described. In the design, the overall protein fold was specified by hydrophobic-polar residue patterning, whereas the bundle oligomerization state, detailed main-chain conformation, and interior side-chain rotamers were engineered by computational enumerations of packing in alternate backbone structures. Main-chain flexibility was incorporated through an algebraic parameterization of the backbone. The designed peptides form alpha-helical dimers, trimers, and tetramers in accord with the design goals. The crystal structure of the tetramer matches the designed structure in atomic detail.


==About this Structure==
High-resolution protein design with backbone freedom.,Harbury PB, Plecs JJ, Tidor B, Alber T, Kim PS Science. 1998 Nov 20;282(5393):1462-7. PMID:9822371<ref>PMID:9822371</ref>
The following page contains interesting information on the relation of 1RH4 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb70_1.html Designer Proteins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RH4 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
High-resolution protein design with backbone freedom., Harbury PB, Plecs JJ, Tidor B, Alber T, Kim PS, Science. 1998 Nov 20;282(5393):1462-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9822371 9822371]
</div>
<div class="pdbe-citations 1rh4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Designer Proteins]]
[[Category: Designer Proteins]]
[[Category: Alber, T.]]
[[Category: Large Structures]]
[[Category: Harbury, P B.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Kim, P S.]]
[[Category: Synthetic construct]]
[[Category: Plecs, J J.]]
[[Category: Alber T]]
[[Category: Tidor, B.]]
[[Category: Harbury PB]]
[[Category: Coiled coil]]
[[Category: Kim PS]]
[[Category: De novo design]]
[[Category: Plecs JJ]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:29:31 2008''
[[Category: Tidor B]]

Latest revision as of 03:26, 21 November 2024

RH4 DESIGNED RIGHT-HANDED COILED COIL TETRAMERRH4 DESIGNED RIGHT-HANDED COILED COIL TETRAMER

Structural highlights

1rh4 is a 1 chain structure with sequence from Synthetic construct. The October 2005 RCSB PDB Molecule of the Month feature on Designer Proteins by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Recent advances in computational techniques have allowed the design of precise side-chain packing in proteins with predetermined, naturally occurring backbone structures. Because these methods do not model protein main-chain flexibility, they lack the breadth to explore novel backbone conformations. Here the de novo design of a family of alpha-helical bundle proteins with a right-handed superhelical twist is described. In the design, the overall protein fold was specified by hydrophobic-polar residue patterning, whereas the bundle oligomerization state, detailed main-chain conformation, and interior side-chain rotamers were engineered by computational enumerations of packing in alternate backbone structures. Main-chain flexibility was incorporated through an algebraic parameterization of the backbone. The designed peptides form alpha-helical dimers, trimers, and tetramers in accord with the design goals. The crystal structure of the tetramer matches the designed structure in atomic detail.

High-resolution protein design with backbone freedom.,Harbury PB, Plecs JJ, Tidor B, Alber T, Kim PS Science. 1998 Nov 20;282(5393):1462-7. PMID:9822371[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Harbury PB, Plecs JJ, Tidor B, Alber T, Kim PS. High-resolution protein design with backbone freedom. Science. 1998 Nov 20;282(5393):1462-7. PMID:9822371

1rh4, resolution 1.90Å

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