View source for 2kbc


==Solution structure of human insulin-like peptide 5 (INSL5)==
<StructureSection load='2kbc' size='340' side='right'caption='[[2kbc]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2kbc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KBC FirstGlance]. <br>
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=2kbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kbc OCA], [https://pdbe.org/2kbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kbc RCSB], [https://www.ebi.ac.uk/pdbsum/2kbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kbc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/INSL5_HUMAN INSL5_HUMAN] May have a role in gut contractility or in thymic development and regulation. Activates RXFP4 with high potency and appears to be the endogenous ligand for this receptor.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
INSL5 (insulin-like peptide 5) is a two-chain peptide hormone related to insulin and relaxin. It was recently discovered through searches of expressed sequence tag databases and, although the full biological significance of INSL5 is still being elucidated, high expression in peripheral tissues such as the colon, as well as in the brain and hypothalamus, suggests roles in gut contractility and neuroendocrine signalling. INSL5 activates the relaxin family peptide receptor 4 with high potency and appears to be the endogenous ligand for this receptor, on the basis of overlapping expression profiles and their apparent co-evolution. In the present study, we have used solution-state NMR to characterize the three-dimensional structure of synthetic human INSL5. The structure reveals an insulin/relaxin-like fold with three helical segments that are braced by three disulfide bonds and enclose a hydrophobic core. Furthermore, we characterized in detail the hydrogen-bond network and electrostatic interactions between charged groups in INSL5 by NMR-monitored temperature and pH titrations and undertook a comprehensive structural comparison with other members of the relaxin family, thus identifying the conserved structural features of the relaxin fold. The B-chain helix, which is the primary receptor-binding site of the relaxins, is longer in INSL5 than in its close relative relaxin-3. As this feature results in a different positioning of the receptor-activation domain Arg(B23) and Trp(B24), it may be an important contributor to the difference in biological activity observed for these two peptides. Overall, the structural studies provide mechanistic insights into the receptor selectivity of this important family of hormones.

Structure of human insulin-like peptide 5 and characterization of conserved hydrogen bonds and electrostatic interactions within the relaxin framework.,Haugaard-Jonsson LM, Hossain MA, Daly NL, Craik DJ, Wade JD, Rosengren KJ Biochem J. 2009 May 1;419(3):619-27. PMID:19178384<ref>PMID:19178384</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kbc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Haugaard-Jonsson LM]]
[[Category: Rosengren KJ]]