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1iml
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(New page: 200px<br /><applet load="1iml" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iml" /> '''CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 ST...)
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Revision as of 15:23, 20 November 2007
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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 with ZN as ligand. 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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