1ieh

<StructureSection load='1ieh' size='340' side='right'caption='[[1ieh]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1ieh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Camelus_glama Camelus glama]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IEH FirstGlance]. <br>

</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=1ieh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ieh OCA], [https://pdbe.org/1ieh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ieh RCSB], [https://www.ebi.ac.uk/pdbsum/1ieh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ieh ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The three-dimensional structure of a llama single-domain antibody BrucD4-4 was established by use of solution NMR spectroscopy. BrucD4-4 has Val, Gly, Leu, and Trp residues at positions 37, 44, 45, and 47, which are considered to be a hallmark to distinguish llama VH from V(H)H fragments at the germline level. In contrast to the murine and human VHs, BrucD4-4 has sufficient solubility, is monomeric in solution, and displays high-quality NMR spectra characteristic of well-structured proteins. Amide proton/deuterium exchange and the (15)N relaxation data showed that BrucD4-4 has a classic protein structure with a well-packed core and comparatively mobile surface loops. The three-dimensional architecture of BrucD4-4 is analogous to that of VHs from murine and human F(v)s and camelid V(H)Hs with two pleated beta-sheets formed by four and five beta-strands. A canonical and undistorted beta-barrel exposes a number of hydrophobic residues into the solvent on the surface of the three-dimensional structure. The eight-residue H3 loop folds over the side chain of Val37 similarly to that in llama V(H)Hs; however, this interaction may be transient due to the H3 conformational flexibility. Overall, the surface characteristics of BrucD4-4 with respect to hydrophobicity appear to lie between the human VH domain from Fv Pot and the llama V(H)H fragment HC-V, which may explain its enhanced solubility allowing NMR structural analysis.

Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface.,Vranken W, Tolkatchev D, Xu P, Tanha J, Chen Z, Narang S, Ni F Biochemistry. 2002 Jul 9;41(27):8570-9. PMID:12093273<ref>PMID:12093273</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 1ieh" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Camelus glama]]

[[Category: Chen, Z]]

[[Category: Narang, S]]

[[Category: Ni, F]]

[[Category: Tanha, J]]

[[Category: Tolkatchev, D]]

[[Category: Vranken, W]]

[[Category: Xu, P]]

[[Category: Two pleated beta-sheet]]