2joo: Difference between revisions
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<StructureSection load='2joo' size='340' side='right'caption='[[2joo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2joo' size='340' side='right'caption='[[2joo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2joo]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2joo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hirme Hirme]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JOO 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=2joo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2joo OCA], [https://pdbe.org/2joo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2joo RCSB], [https://www.ebi.ac.uk/pdbsum/2joo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2joo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/HIRV1_HIRME HIRV1_HIRME]] Hirudin is a potent thrombin-specific protease inhibitor. It forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen.<ref>PMID:17585879</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 20:56, 20 October 2021
The NMR Solution Structure of Recombinant RGD-hirudinThe NMR Solution Structure of Recombinant RGD-hirudin
Structural highlights
Function[HIRV1_HIRME] Hirudin is a potent thrombin-specific protease inhibitor. It forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen.[1] 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 PubMedThe solution structure of a new recombinant RGD-hirudin, which has the activities of anti-thrombin and anti-platelet aggregation, was determined by (1)H nuclear magnetic resonance spectroscopy and compared with the conformations of recombinant wild-type hirudin and hirudin (variant 2, Lys47) of the hirudin thrombin complex. On the basis of total 1284 distance and dihedral angle constraints derived from a series of NMR spectra, 20 conformers were computed with ARIA/CNS programs. The structure of residues 3-30 and 37-48 form a molecular core with two antiparallel beta-sheets as the other two hirudins. However, significant differences were found in the surface electrostatic charge distributions among the three hirudins, especially in the RGD segment of recombinant RGD-hirudin. This difference may be greatly beneficial to its additional function of anti-platelet aggregation. The difference in extended C-terminal makes its both ionic and hydrophobic interactions with the fibrinogen recognition exosite of thrombin more effective. The NMR solution structure of recombinant RGD-hirudin.,Song X, Mo W, Liu X, Zhu L, Yan X, Song H, Dai L Biochem Biophys Res Commun. 2007 Aug 17;360(1):103-8. Epub 2007 Jun 13. PMID:17585879[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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