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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[[Image:1iml.gif|left|200px]]<br /><applet load="1iml" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1iml" />
 
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'''CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES'''<br />
 
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==Overview==
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==CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES==
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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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<StructureSection load='1iml' size='340' side='right'caption='[[1iml]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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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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1IML is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IML OCA].
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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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<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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==Reference==
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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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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8632452 8632452]
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</table>
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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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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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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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<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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</jmolCheckbox>
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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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:30:21 2007''
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CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES

PDB ID 1iml

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