1iml
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1iml.gif|left|200px]] | + | [[Image:1iml.gif|left|200px]] |
| - | + | ||
| - | '''CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1iml |SIZE=350|CAPTION= <scene name='initialview01'>1iml</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= CRIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10117 Rattus rattus]) | ||
| + | }} | ||
| + | |||
| + | '''CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1IML is a [ | + | 1IML is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IML OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8632452 8632452] |
[[Category: Rattus rattus]] | [[Category: Rattus rattus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 23: | Line 32: | ||
[[Category: metal-binding protein]] | [[Category: metal-binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:52:15 2008'' |
Revision as of 09:52, 20 March 2008
| |||||||
| Ligands: | |||||||
| Gene: | CRIP (Rattus rattus) | ||||||
| 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
Page seeded by OCA on Thu Mar 20 11:52:15 2008
