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1iml

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[[Image:1iml.gif|left|200px]]
 
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{{Structure
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==CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES==
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|PDB= 1iml |SIZE=350|CAPTION= <scene name='initialview01'>1iml</scene>
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<StructureSection load='1iml' size='340' side='right'caption='[[1iml]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1iml]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IML FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= CRIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10117 Rattus rattus])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iml OCA], [https://pdbe.org/1iml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iml RCSB], [https://www.ebi.ac.uk/pdbsum/1iml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iml ProSAT]</span></td></tr>
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</table>
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'''CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES'''
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== Function ==
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[https://www.uniprot.org/uniprot/CRIP1_RAT CRIP1_RAT] Seems to have a role in zinc absorption and may function as an intracellular zinc transport protein.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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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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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/im/1iml_consurf.spt"</scriptWhenChecked>
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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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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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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]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1iml ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Rattus rattus]]
[[Category: Rattus rattus]]
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[[Category: Single protein]]
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[[Category: Beckerle MC]]
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[[Category: Beckerle, M C.]]
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[[Category: Kosa JL]]
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[[Category: Kosa, J L.]]
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[[Category: Louis HA]]
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[[Category: Louis, H A.]]
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[[Category: Perez-Alvarado GC]]
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[[Category: Perez-Alvarado, G C.]]
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[[Category: Summers MF]]
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[[Category: Summers, M F.]]
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[[Category: Winge DR]]
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[[Category: Winge, D R.]]
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[[Category: ZN]]
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[[Category: lim domain protein]]
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[[Category: metal-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:52:15 2008''
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Current revision

CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES

PDB ID 1iml

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