2i18

<StructureSection load='2i18' size='340' side='right'caption='[[2i18]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2i18]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2ev7 2ev7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I18 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2I18 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LA:LANTHANUM+(III)+ION'>LA</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jfk|1jfk]], [[1jfj|1jfj]]</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=2i18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i18 OCA], [http://pdbe.org/2i18 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i18 RCSB], [http://www.ebi.ac.uk/pdbsum/2i18 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2i18 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CALBP_ENTHI CALBP_ENTHI]] Could play a role in the transduction of secondary messages on binding of calcium.

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== Publication Abstract from PubMed ==

Lanthanide ions (Ln(3+)), which have ionic radii similar to those of Ca(2+), can displace the latter in a calcium binding protein, without affecting its tertiary structure. The paramagnetic Ln(3+) possesses large anisotropic magnetic susceptibilities and produce pseudocontact shifts (PCSs), which have r(-3) dependence. The PCS can be seen for spins as far as 45 A from the paramagnetic ion. They aid in structure refinement of proteins by providing long-range distance constraints. Besides, they can be used to determine the interdomain orientation in multidomain proteins. This is particularly important in the context of a calcium binding protein from Entamoeba histolytica (EhCaBP), which consists of two globular domains connected by a flexible linker region containing 8 residues. As a first step to obtain the interdomain orientation in EhCaBP, a suite of 2D and 3D heteronuclear experiments were recorded on EhCaBP by displacing calcium with Ce(3+), Ho(3+), Er(3+), Tm(3+), Dy(3+), and Yb(3+) ions in separate experiments, and the PCS of (1)H(N) and (15)N spins were measured. Such data have been used in the refinement of the individual domain structures of the protein in parallel with the calculation of the respective magnetic anisotropy tensorial values, which differ substantially (2.1-2.8 times) from what is found in other Ca(2+) binding loops. This study provides a structural basis for such variations in the magnetic anisotropy tensorial values.

Structural basis for the observed differential magnetic anisotropic tensorial values in calcium binding proteins.,Mustafi SM, Mukherjee S, Chary KV, Cavallaro G Proteins. 2006 Nov 15;65(3):656-69. PMID:16981203<ref>PMID:16981203</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2i18" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Chary, K V.R]]

[[Category: Mukherjee, S]]

[[Category: Mustafi, S M]]

[[Category: Metal binding protein]]