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1iml

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[[Image:1iml.gif|left|200px]]
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{{STRUCTURE_1iml| PDB=1iml | SCENE= }}
{{STRUCTURE_1iml| PDB=1iml | SCENE= }}
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'''CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES'''
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===CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES===
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==Overview==
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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 &lt; or = 0.03 angstrom and penalties (squared sum of distance violations) of &lt; 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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8632452 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8632452}}
==About this Structure==
==About this Structure==
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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].
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1IML is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IML OCA].
==Reference==
==Reference==
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[[Category: Lim domain protein]]
[[Category: Lim domain protein]]
[[Category: Metal-binding protein]]
[[Category: Metal-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:09:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:33:16 2008''

Revision as of 10:33, 1 July 2008

Image:1iml.png

Template:STRUCTURE 1iml

CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES

Template:ABSTRACT PUBMED 8632452

About this Structure

1IML is a Single protein structure of sequence from Rattus rattus. Full experimental 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 Tue Jul 1 13:33:16 2008

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