1wo3: Difference between revisions

Revision as of 07:53, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1wo3.png

Template:STRUCTURE 1wo3

Solution structure of Minimal Mutant 1 (MM1): Multiple alanine mutant of non-native CHANCE domainSolution structure of Minimal Mutant 1 (MM1): Multiple alanine mutant of non-native CHANCE domain

Template:ABSTRACT PUBMED 15698569

About this StructureAbout this Structure

1WO3 is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

Assessment of the robustness of a serendipitous zinc binding fold: mutagenesis and protein grafting., Sharpe BK, Liew CK, Kwan AH, Wilce JA, Crossley M, Matthews JM, Mackay JP, Structure. 2005 Feb;13(2):257-66. PMID:15698569

Page seeded by OCA on Tue Jul 29 07:53:24 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1wo3.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1wo3|  PDB=1wo3  |  SCENE=  }}
-'''Solution structure of Minimal Mutant 1 (MM1): Multiple alanine mutant of non-native CHANCE domain'''
+===Solution structure of Minimal Mutant 1 (MM1): Multiple alanine mutant of non-native CHANCE domain===
-==Overview==
+<!--
-Zinc binding motifs have received much attention in the area of protein design. Here, we have tested the suitability of a recently discovered nonnative zinc binding structure as a protein design scaffold. A series of multiple alanine mutants was created to investigate the minimal requirements for folding, and solution structures of these mutants showed that the original fold was maintained, despite changes in approximately 50% of the sequence. We next attempted to transplant binding faces from chosen bimolecular interactions onto one of these mutants, and many of the resulting "chimeras" were shown to adopt a native-like fold. These results both highlight the robust nature of small zinc binding domains and underscore the complexity of designing functional proteins, even using such small, highly ordered scaffolds as templates.
+The line below this paragraph, {{ABSTRACT_PUBMED_15698569}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15698569 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15698569}}
 ==About this Structure==
-WO3 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WO3 OCA].
+WO3 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WO3 OCA].
 ==Reference==
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 [[Category: Protein design]]
 [[Category: Zinc finger]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:56:08 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:53:24 2008''