2kra: Difference between revisions
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<StructureSection load='2kra' size='340' side='right'caption='[[2kra]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2kra' size='340' side='right'caption='[[2kra]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2kra]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2kra]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bomva Bomva]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KRA FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=2kra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kra OCA], [https://pdbe.org/2kra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kra RCSB], [https://www.ebi.ac.uk/pdbsum/2kra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kra ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 10:35, 2 February 2022
Solution structure of Bv8Solution structure of Bv8
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBv8, a 77-residue protein isolated from frogs, is the prototypic member of the prokineticin family of cytokines. Prokineticins (PKs) have only recently been identified in vertebrates (including humans), and they are believed to be involved in a number of key physiological processes, such as angiogenesis, neurogenesis, nociception, and tissue development. We used a combination of Boc solid-phase peptide synthesis, native chemical ligation, and in vitro protein folding to establish robust chemical access to this molecule. Synthetic Bv8 was obtained in good yield and exhibited full activity in a human neuroblastoma cell line and rat dorsal root ganglion (DRG) neurons. The 3D structure of the synthetic protein was determined by using NMR spectroscopy and it was found to be homologous with that of mamba intestinal toxin 1, which is the only other known prokineticin structure. Analysis of a truncated mutant lacking five residues at the N terminus that are critical for receptor binding and activation showed no perturbation to the core protein structure. Together with the functional data, this suggests that receptor binding is likely to be a highly cooperative process possibly involving major allosterically driven structural rearrangements. The facile and efficient synthesis presented here will enable preparation of unique chemical analogues of prokineticins, which should be powerful tools for modulating the structure and function of prokineticins and their receptors, and studying the many physiological processes that have been linked to them. Chemical synthesis and structure of the prokineticin Bv8.,Morales RA, Daly NL, Vetter I, Mobli M, Napier IA, Craik DJ, Lewis RJ, Christie MJ, King GF, Alewood PF, Durek T Chembiochem. 2010 Sep 3;11(13):1882-8. doi: 10.1002/cbic.201000330. PMID:20677202[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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