1iml
From Proteopedia
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|PDB= 1iml |SIZE=350|CAPTION= <scene name='initialview01'>1iml</scene> | |PDB= 1iml |SIZE=350|CAPTION= <scene name='initialview01'>1iml</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= CRIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10117 Rattus rattus]) | |GENE= CRIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10117 Rattus rattus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iml OCA], [http://www.ebi.ac.uk/pdbsum/1iml PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iml RCSB]</span> | ||
}} | }} | ||
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[[Category: Summers, M F.]] | [[Category: Summers, M F.]] | ||
[[Category: Winge, D R.]] | [[Category: Winge, D R.]] | ||
| - | [[Category: ZN]] | ||
[[Category: lim domain protein]] | [[Category: lim domain protein]] | ||
[[Category: metal-binding protein]] | [[Category: metal-binding protein]] | ||
| - | ''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 21:21:47 2008'' |
Revision as of 18:21, 30 March 2008
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| Ligands: | |||||||
| Gene: | CRIP (Rattus rattus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES
Overview
LIM domains are Zn-binding arrays found in a number of proteins involved in the control of cell differentiation, including several developmentally regulated transcription factors and a human proto-oncogene product. The rat cysteine-rich intestinal protein, CRIP, is a 76-residue polypeptide which contains a LIM motif. The solution structure of CRIP has been determined by homonuclear and 1H-15N heteronuclear correlated nuclear magnetic resonance spectroscopy. Structures with individual distance violations of < or = 0.03 angstrom and penalties (squared sum of distance violations) of < or = 0.06 angstrom2 were generated with a total of 500 nuclear Overhauser effect (NOE)-derived distance restraints (averaging 15.6 restraints per refined residue). Superposition of backbone heavy atoms of ordered residues relative to mean atom positions is achieved with pairwise rms deviations of 0.54(+/-0.14) angstrom. As observed previously for a peptide with the sequence of the C-terminal LIM domain from the avian cysteine-rich protein, CRP (cCRP-LIM2), CRIP binds two equivalents of zinc, forming N-terminal CCHC (Cys3, Cys6, His24, Cys27) and C-terminal CCCC (Cys30, Cys33, Cys51, Cys55) modules. The CCHC and CCCC modules in CRIP contain two orthogonally-arrayed antiparallel beta-sheets. The C-terminal end of the CCHC module contains a tight turn and the C terminus of the CCCC module forms an alpha-helix. The modules pack via hydrophobic interactions, forming a compact structure that is similar to that observed for cCRP-LIM2. The most significant differences between the structures occur at the CCHC module-CCCC module interface, which results in a difference in the relative orientations of the modules, and at the C terminus where the alpha-helix appears to be packed more tightly against the preceding antiparallel beta-sheet. The greater abundance of NOE information obtained for CRIP relative to cCRP-LIM2, combined with the analysis of J-coupling and proton chemical shift data, have allowed a more detailed evaluation of the molecular level interactions that stabilize the fold of the LIM motif.
About this Structure
1IML is a Single protein structure of sequence from Rattus rattus. Full crystallographic information is available from OCA.
Reference
Structure of the cysteine-rich intestinal protein, CRIP., Perez-Alvarado GC, Kosa JL, Louis HA, Beckerle MC, Winge DR, Summers MF, J Mol Biol. 1996 Mar 22;257(1):153-74. PMID:8632452
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