1liq
From Proteopedia
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|PDB= 1liq |SIZE=350|CAPTION= <scene name='initialview01'>1liq</scene> | |PDB= 1liq |SIZE=350|CAPTION= <scene name='initialview01'>1liq</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1liq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1liq OCA], [http://www.ebi.ac.uk/pdbsum/1liq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1liq RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=303900 303900]], Colorblindness, protan OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=303900 303900]], Rubenstein-Taybi syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600140 600140]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Newton, A.]] | [[Category: Newton, A.]] | ||
[[Category: Sharpe, B K.]] | [[Category: Sharpe, B K.]] | ||
| - | [[Category: ZN]] | ||
[[Category: protein design]] | [[Category: protein design]] | ||
[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:03:16 2008'' |
Revision as of 19:03, 30 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Non-native Solution Structure of a fragment of the CH1 domain of CBP
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.
About this Structure
1LIQ is a Single protein structure of sequence from [1]. 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
Page seeded by OCA on Sun Mar 30 22:03:16 2008
