1bds

From Proteopedia

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Current revision

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

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

↑ 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
↑ 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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bds"

Categories: Anemonia sulcata | Large Structures | Clore GM | Driscoll PC | Gronenborn AM

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1bds.png|left|200px]]
-<!--
+==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==
-The line below this paragraph, containing "STRUCTURE_1bds", creates the "Structure Box" on the page.
+<StructureSection load='1bds' size='340' side='right'caption='[[1bds]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
-{{STRUCTURE_1bds|  PDB=1bds  |  SCENE=  }}
+</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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_2566326}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1bds" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 2566326 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_2566326}}
+__TOC__
+</StructureSection>
-==About this Structure==
-BDS is a [[Single protein]] structure of 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].
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/2566326 2566326]
 [[Category: Anemonia sulcata]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Clore, G M.]]
+[[Category: Clore GM]]
-[[Category: Driscoll, P C.]]
+[[Category: Driscoll PC]]
-[[Category: Gronenborn, A M.]]
+[[Category: Gronenborn AM]]
-[[Category: Anti-hypertensive]]
-[[Category: Anti-viral protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:55:21 2008''

1bds

From Proteopedia

Current revision

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

Structural highlights

Function

Publication Abstract from PubMed

References

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