2i99

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[[Image:2i99.jpg|left|200px]]<br /><applet load="2i99" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2i99, resolution 2.600&Aring;" />
 
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'''Crystal structure of human Mu_crystallin at 2.6 Angstrom'''<br />
 
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==Overview==
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==Crystal structure of human Mu_crystallin at 2.6 Angstrom==
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Human cytosolic 3,5,3'-triiodo-L-thyronine-binding protein, also called, mu-crystallin or CRYM, plays important physiological roles in transporting, 3,5,3'-triiodo-L-thyronine (T(3)) into nuclei and regulating, thyroid-hormone-related gene expression. The crystal structure of human, CRYM's bacterial homolog Pseudomonas putida ornithine cyclodeaminase and, Archaeoglobus fulgidus alanine dehydrogenase have been available, but no, CRYM structure has been reported. Here, we report the crystal structure of, human CRYM bound with NADPH refined to 2.6 A, and there is one dimer in, the asymmetric unit. The structure contains two domains: a Rossmann, fold-like NADPH-binding domain and a dimerization domain. Different, conformations of the loop Arg83-His92 have been observed in two monomers, of human CRYM in the same asymmetric unit. The peptide bond of Val89-Pro90, is a trans-configuration in one monomer but a cis-configuration in the, other. A detailed comparison of the human mu-crystallin structure with its, structurally characterized homologs including the overall comparison and, superposition of active sites was conducted. Finally, a putative, T(3)-binding site in human CRYM is proposed based on comparison with, structural homologs.
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<StructureSection load='2i99' size='340' side='right'caption='[[2i99]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2i99]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I99 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
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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=2i99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i99 OCA], [https://pdbe.org/2i99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i99 RCSB], [https://www.ebi.ac.uk/pdbsum/2i99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i99 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CRYM_HUMAN CRYM_HUMAN] Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine and access to its nuclear receptors.<ref>PMID:21332720</ref>
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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/i9/2i99_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=2i99 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human cytosolic 3,5,3'-triiodo-L-thyronine-binding protein, also called mu-crystallin or CRYM, plays important physiological roles in transporting 3,5,3'-triiodo-L-thyronine (T(3)) into nuclei and regulating thyroid-hormone-related gene expression. The crystal structure of human CRYM's bacterial homolog Pseudomonas putida ornithine cyclodeaminase and Archaeoglobus fulgidus alanine dehydrogenase have been available, but no CRYM structure has been reported. Here, we report the crystal structure of human CRYM bound with NADPH refined to 2.6 A, and there is one dimer in the asymmetric unit. The structure contains two domains: a Rossmann fold-like NADPH-binding domain and a dimerization domain. Different conformations of the loop Arg83-His92 have been observed in two monomers of human CRYM in the same asymmetric unit. The peptide bond of Val89-Pro90 is a trans-configuration in one monomer but a cis-configuration in the other. A detailed comparison of the human mu-crystallin structure with its structurally characterized homologs including the overall comparison and superposition of active sites was conducted. Finally, a putative T(3)-binding site in human CRYM is proposed based on comparison with structural homologs.
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==Disease==
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Crystal structure of human micro-crystallin complexed with NADPH.,Cheng Z, Sun L, He J, Gong W Protein Sci. 2007 Feb;16(2):329-35. PMID:17242435<ref>PMID:17242435</ref>
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Known disease associated with this structure: Deafness, autosomal dominant 40 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=123740 123740]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2I99 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NDP:'>NDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I99 OCA].
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</div>
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<div class="pdbe-citations 2i99" style="background-color:#fffaf0;"></div>
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==Reference==
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== References ==
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Crystal structure of human micro-crystallin complexed with NADPH., Cheng Z, Sun L, He J, Gong W, Protein Sci. 2007 Feb;16(2):329-35. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17242435 17242435]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cheng, Z.]]
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[[Category: Cheng Z]]
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[[Category: Gong, W.]]
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[[Category: Gong W]]
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[[Category: He, J.]]
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[[Category: He J]]
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[[Category: Sun, L.]]
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[[Category: Sun L]]
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[[Category: NDP]]
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[[Category: mu_crystallin]]
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[[Category: thyroid hormine binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:35:18 2008''
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Current revision

Crystal structure of human Mu_crystallin at 2.6 Angstrom

PDB ID 2i99

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