1liq
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(New page: 200px<br /> <applet load="1liq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1liq" /> '''Non-native Solution Structure of a fragment...)
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Revision as of 15:55, 12 November 2007
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Non-native Solution Structure of a fragment of the CH1 domain of CBP
Contents |
Overview
Many different zinc binding modules have been identified. Their abundance, and variety suggests that the formation of zinc binding folds might be, relatively common. We have determined the structure of CH1(1), a, 27-residue peptide derived from the first cysteine/histidine-rich region, (CH1) of CREB binding protein (CBP). This peptide forms a highly ordered, zinc-dependent fold that is distinct from known folds. The structure, differs from a subsequently determined structure of a larger region from, the CH3 region of CBP, and the CH1(1) fold probably represents a, nonphysiologically active form. Despite this, the fold is thermostable and, tolerant to both multiple alanine mutations and changes in the zinc-ligand, spacing. Our data support the idea that zinc binding domains may arise, frequently. Additionally, such structures may prove useful as scaffolds, for protein design, given their stability and robustness.
Disease
Known diseases associated with this structure: Blue-cone monochromacy OMIM:[303900], Colorblindness, protan OMIM:[303900], Rubenstein-Taybi syndrome OMIM:[600140]
About this Structure
1LIQ is a Single protein structure of sequence from [1] with ZN as ligand. Full crystallographic information is available from OCA.
Reference
A new zinc binding fold underlines the versatility of zinc binding modules in protein evolution., Sharpe BK, Matthews JM, Kwan AH, Newton A, Gell DA, Crossley M, Mackay JP, Structure. 2002 May;10(5):639-48. PMID:12015147
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