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==CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES==
==CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES==
<StructureSection load='1iml' size='340' side='right' caption='[[1iml]], [[NMR_Ensembles_of_Models | 48 NMR models]]' scene=''>
<StructureSection load='1iml' size='340' side='right'caption='[[1iml]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1iml]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Black_rat Black rat]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IML FirstGlance]. <br>
<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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CRIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10117 Black rat])</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iml OCA], [http://pdbe.org/1iml PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iml RCSB], [http://www.ebi.ac.uk/pdbsum/1iml PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iml ProSAT]</span></td></tr>
<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>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CRIP1_MOUSE CRIP1_MOUSE]] Seems to have a role in zinc absorption and may function as an intracellular zinc transport protein.  
[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/im/1iml_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/im/1iml_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 20: Line 20:
</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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:8632452</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1iml" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Black rat]]
[[Category: Large Structures]]
[[Category: Beckerle, M C]]
[[Category: Rattus rattus]]
[[Category: Kosa, J L]]
[[Category: Beckerle MC]]
[[Category: Louis, H A]]
[[Category: Kosa JL]]
[[Category: Perez-Alvarado, G C]]
[[Category: Louis HA]]
[[Category: Summers, M F]]
[[Category: Perez-Alvarado GC]]
[[Category: Winge, D R]]
[[Category: Summers MF]]
[[Category: Lim domain protein]]
[[Category: Winge DR]]
[[Category: Metal binding protein]]
[[Category: Metal-binding protein]]

Latest revision as of 07:48, 3 April 2024

CYSTEINE RICH INTESTINAL PROTEIN, NMR, 48 STRUCTURES

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