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3ebx

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Revision as of 07:13, 29 November 2017

REFINEMENT AT 1.4 ANGSTROMS RESOLUTION OF A MODEL OF ERABUTOXIN B. TREATMENT OF ORDERED SOLVENT AND DISCRETE DISORDER

Structural highlights

3ebx is a 1 chain structure with sequence from Black-banded sea krait. This structure supersedes the now removed PDB entry 2ebx. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	5ebx
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NXSB_PSSEM] Binds with high affinity to muscular nicotinic acetylcholine receptors (nAChRs), and with low affinity to neuronal alpha-7 nAChRs and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site.^[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 latter stages in the refinement of the protein erabutoxin b are described. The crystal structure of the 62-residue protein has been refined to a conventional R factor of 0.144 by stereochemically restrained least-squares methods using diffraction data to a limit of 1.4 A spacings. Emphasis was placed on determining as accurately as possible the solvent structure and the structures of heterogeneous groups in the protein. The final model includes two conformers for each of seven side chains and for an octapeptide segment. A total of 111 sites for water molecules have been located as well as one sulfate ion with a total of 68 site occupancies. 65 of the solvent sites overlap either with protein atoms belonging to groups in two alternative conformations or with other solvent sites. Dual protein conformers and overlapping solvent sites were both included in the least-squares refinement. Individual thermal and occupancy parameters were refined for solvent molecules. An analysis of these parameters has provided useful structural information.

Refinement at 1.4 A resolution of a model of erabutoxin b: treatment of ordered solvent and discrete disorder.,Smith JL, Corfield PW, Hendrickson WA, Low BW Acta Crystallogr A. 1988 May 1;44 ( Pt 3):357-68. PMID:3272151^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Servent D, Winckler-Dietrich V, Hu HY, Kessler P, Drevet P, Bertrand D, Menez A. Only snake curaremimetic toxins with a fifth disulfide bond have high affinity for the neuronal alpha7 nicotinic receptor. J Biol Chem. 1997 Sep 26;272(39):24279-86. PMID:9305882
↑ Smith JL, Corfield PW, Hendrickson WA, Low BW. Refinement at 1.4 A resolution of a model of erabutoxin b: treatment of ordered solvent and discrete disorder. Acta Crystallogr A. 1988 May 1;44 ( Pt 3):357-68. PMID:3272151

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ebx"

@@ Line 1: / Line 1: @@
 ==REFINEMENT AT 1.4 ANGSTROMS RESOLUTION OF A MODEL OF ERABUTOXIN B. TREATMENT OF ORDERED SOLVENT AND DISCRETE DISORDER==
 <StructureSection load='3ebx' size='340' side='right' caption='[[3ebx]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ebx|5ebx]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ebx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ebx OCA], [http://pdbe.org/3ebx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ebx RCSB], [http://www.ebi.ac.uk/pdbsum/3ebx PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ebx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ebx OCA], [http://pdbe.org/3ebx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ebx RCSB], [http://www.ebi.ac.uk/pdbsum/3ebx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ebx ProSAT]</span></td></tr>
 </table>
 == Function ==

3ebx

From Proteopedia

Revision as of 07:13, 29 November 2017

REFINEMENT AT 1.4 ANGSTROMS RESOLUTION OF A MODEL OF ERABUTOXIN B. TREATMENT OF ORDERED SOLVENT AND DISCRETE DISORDER

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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