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2joo

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Revision as of 17:56, 20 October 2021

The NMR Solution Structure of Recombinant RGD-hirudin

Structural highlights

2joo is a 1 chain structure with sequence from Hirme. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

The 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.

References

↑ Song X, Mo W, Liu X, Zhu L, Yan X, Song H, Dai L. The NMR solution structure of recombinant RGD-hirudin. Biochem Biophys Res Commun. 2007 Aug 17;360(1):103-8. Epub 2007 Jun 13. PMID:17585879 doi:10.1016/j.bbrc.2007.06.014
↑ Song X, Mo W, Liu X, Zhu L, Yan X, Song H, Dai L. The NMR solution structure of recombinant RGD-hirudin. Biochem Biophys Res Commun. 2007 Aug 17;360(1):103-8. Epub 2007 Jun 13. PMID:17585879 doi:10.1016/j.bbrc.2007.06.014

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2joo"

@@ Line 3: / Line 3: @@
 <StructureSection load='2joo' size='340' side='right'caption='[[2joo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2joo]] is a 1 chain structure with sequence from [http://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 [http://proteopedia.org/fgij/fg.htm?mol=2JOO FirstGlance]. <br>
+<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'>[http://proteopedia.org/fgij/fg.htm?mol=2joo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2joo OCA], [http://pdbe.org/2joo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2joo RCSB], [http://www.ebi.ac.uk/pdbsum/2joo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2joo ProSAT]</span></td></tr>
+</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>
 == Function ==
-[[http://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>
+[[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

2joo

From Proteopedia

Revision as of 17:56, 20 October 2021

The NMR Solution Structure of Recombinant RGD-hirudin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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