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[[Image:1mhu.gif|left|200px]]


{{Structure
==THE THREE-DIMENSIONAL STRUCTURE OF HUMAN [113CD7] METALLOTHIONEIN-2 IN SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY==
|PDB= 1mhu |SIZE=350|CAPTION= <scene name='initialview01'>1mhu</scene>
<StructureSection load='1mhu' size='340' side='right'caption='[[1mhu]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>
<table><tr><td colspan='2'>[[1mhu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MHU FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhu OCA], [https://pdbe.org/1mhu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mhu RCSB], [https://www.ebi.ac.uk/pdbsum/1mhu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mhu ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mhu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhu OCA], [http://www.ebi.ac.uk/pdbsum/1mhu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mhu RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/MT2_HUMAN MT2_HUMAN] Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
 
<div style="background-color:#fffaf0;">
'''THE THREE-DIMENSIONAL STRUCTURE OF HUMAN [113CD7] METALLOTHIONEIN-2 IN SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY'''
== Publication Abstract from PubMed ==
 
 
==Overview==
The three-dimensional structure of human [113Cd7]metallothionein-2 was determined by nuclear magnetic resonance spectroscopy in solution. Sequence-specific 1H resonance assignments were obtained using the sequential assignment method. The input for the structure calculations consisted of the metal-cysteine co-ordinative bonds identified with heteronuclear correlation spectroscopy, 1H-1H distance constraints from nuclear Overhauser enhancement spectroscopy, and spin-spin coupling constants 3JHN alpha and 3J alpha beta. The molecule consists of two domains, the beta-domain including amino acid residues 1 to 30 and three metal ions, and the alpha-domain including residues 31 to 61 and four metal ions. The nuclear magnetic resonance data present no evidence for a preferred relative orientation of the two domains. The polypeptide-to-metal co-ordinative bonds in human metallothionein-2 are identical to those in the previously determined solution structures of rat metallothionein-2 and rabbit metallothionein-2a, and the polypeptide conformations in the three proteins are also closely similar.
The three-dimensional structure of human [113Cd7]metallothionein-2 was determined by nuclear magnetic resonance spectroscopy in solution. Sequence-specific 1H resonance assignments were obtained using the sequential assignment method. The input for the structure calculations consisted of the metal-cysteine co-ordinative bonds identified with heteronuclear correlation spectroscopy, 1H-1H distance constraints from nuclear Overhauser enhancement spectroscopy, and spin-spin coupling constants 3JHN alpha and 3J alpha beta. The molecule consists of two domains, the beta-domain including amino acid residues 1 to 30 and three metal ions, and the alpha-domain including residues 31 to 61 and four metal ions. The nuclear magnetic resonance data present no evidence for a preferred relative orientation of the two domains. The polypeptide-to-metal co-ordinative bonds in human metallothionein-2 are identical to those in the previously determined solution structures of rat metallothionein-2 and rabbit metallothionein-2a, and the polypeptide conformations in the three proteins are also closely similar.


==About this Structure==
Three-dimensional structure of human [113Cd7]metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy.,Messerle BA, Schaffer A, Vasak M, Kagi JH, Wuthrich K J Mol Biol. 1990 Aug 5;214(3):765-79. PMID:2388267<ref>PMID:2388267</ref>
1MHU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHU OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Three-dimensional structure of human [113Cd7]metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy., Messerle BA, Schaffer A, Vasak M, Kagi JH, Wuthrich K, J Mol Biol. 1990 Aug 5;214(3):765-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2388267 2388267]
</div>
<div class="pdbe-citations 1mhu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Braun, W.]]
[[Category: Braun W]]
[[Category: Kaegi, J H.R.]]
[[Category: Kaegi JHR]]
[[Category: Messerle, B A.]]
[[Category: Messerle BA]]
[[Category: Schaeffer, A.]]
[[Category: Schaeffer A]]
[[Category: Vasak, M.]]
[[Category: Vasak M]]
[[Category: Wuthrich, K.]]
[[Category: Wuthrich K]]
[[Category: metallothionein]]
 
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Retrieved from "https://proteopedia.org/1mhu"