1bds: Difference between revisions

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[[Image:1bds.png|left|200px]]


{{STRUCTURE_1bds| PDB=1bds |  SCENE= }}
==DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE ANTIHYPERTENSIVE AND ANTIVIRAL PROTEIN BDS-I FROM THE SEA ANEMONE ANEMONIA SULCATA. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING==
<StructureSection load='1bds' size='340' side='right'caption='[[1bds]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bds]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anemonia_sulcata Anemonia sulcata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BDS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=1bds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bds OCA], [https://pdbe.org/1bds PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bds RCSB], [https://www.ebi.ac.uk/pdbsum/1bds PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bds ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BDS1_ANESU BDS1_ANESU] Blocks specifically the Kv3.4/KCNC4 potassium channel. Reduces blood pressure.<ref>PMID:9506974</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata has been determined on the basis of 489 interproton and 24 hydrogen-bonding distance restraints supplemented by 23 phi backbone and 21 chi 1 side-chain torsion angle restraints derived from nuclear magnetic resonance (NMR) measurements. A total of 42 structures is calculated by a hybrid metric matrix distance geometry-dynamical simulated annealing approach. Both the backbone and side-chain atom positions are well defined. The average atomic rms difference between the 42 individual SA structures and the mean structure obtained by averaging their coordinates is 0.67 +/- 0.12 A for the backbone atoms and 0.90 +/- 0.17 A for all atoms. The core of the protein is formed by a triple-stranded antiparallel beta-sheet composed of residues 14-16 (strand 1), 30-34 (strand 2), and 37-41 (strand 3) with an additional mini-antiparallel beta-sheet at the N-terminus (residues 6-9). The first and second strands of the triple-stranded antiparallel beta-sheet are connected by a long exposed loop (residues 17-30). A number of side-chain interactions are discussed in light of the structure.


===DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE ANTIHYPERTENSIVE AND ANTIVIRAL PROTEIN BDS-I FROM THE SEA ANEMONE ANEMONIA SULCATA. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING===
Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing.,Driscoll PC, Gronenborn AM, Beress L, Clore GM Biochemistry. 1989 Mar 7;28(5):2188-98. PMID:2566326<ref>PMID:2566326</ref>


{{ABSTRACT_PUBMED_2566326}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 1bds" style="background-color:#fffaf0;"></div>
[[1bds]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anemonia_sulcata Anemonia sulcata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BDS OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:002566326</ref><ref group="xtra">PMID:011734033</ref><references group="xtra"/>
</StructureSection>
[[Category: Anemonia sulcata]]
[[Category: Anemonia sulcata]]
[[Category: Clore, G M.]]
[[Category: Large Structures]]
[[Category: Driscoll, P C.]]
[[Category: Clore GM]]
[[Category: Gronenborn, A M.]]
[[Category: Driscoll PC]]
[[Category: Anti-hypertensive]]
[[Category: Gronenborn AM]]
[[Category: Anti-viral protein]]

Latest revision as of 09:25, 30 October 2024

DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE ANTIHYPERTENSIVE AND ANTIVIRAL PROTEIN BDS-I FROM THE SEA ANEMONE ANEMONIA SULCATA. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALINGDETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE ANTIHYPERTENSIVE AND ANTIVIRAL PROTEIN BDS-I FROM THE SEA ANEMONE ANEMONIA SULCATA. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING

Structural highlights

1bds is a 1 chain structure with sequence from Anemonia sulcata. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 1 model
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BDS1_ANESU Blocks specifically the Kv3.4/KCNC4 potassium channel. Reduces blood pressure.[1]

Publication Abstract from PubMed

The three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata has been determined on the basis of 489 interproton and 24 hydrogen-bonding distance restraints supplemented by 23 phi backbone and 21 chi 1 side-chain torsion angle restraints derived from nuclear magnetic resonance (NMR) measurements. A total of 42 structures is calculated by a hybrid metric matrix distance geometry-dynamical simulated annealing approach. Both the backbone and side-chain atom positions are well defined. The average atomic rms difference between the 42 individual SA structures and the mean structure obtained by averaging their coordinates is 0.67 +/- 0.12 A for the backbone atoms and 0.90 +/- 0.17 A for all atoms. The core of the protein is formed by a triple-stranded antiparallel beta-sheet composed of residues 14-16 (strand 1), 30-34 (strand 2), and 37-41 (strand 3) with an additional mini-antiparallel beta-sheet at the N-terminus (residues 6-9). The first and second strands of the triple-stranded antiparallel beta-sheet are connected by a long exposed loop (residues 17-30). A number of side-chain interactions are discussed in light of the structure.

Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing.,Driscoll PC, Gronenborn AM, Beress L, Clore GM Biochemistry. 1989 Mar 7;28(5):2188-98. PMID:2566326[2]

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

References

  1. ↑ Diochot S, Schweitz H, Beress L, Lazdunski M. Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4. J Biol Chem. 1998 Mar 20;273(12):6744-9. PMID:9506974
  2. ↑ Driscoll PC, Gronenborn AM, Beress L, Clore GM. Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry. 1989 Mar 7;28(5):2188-98. PMID:2566326
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