1bds: Difference between revisions
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==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== | ||
<StructureSection load='1bds' size='340' side='right'caption='[[1bds | <StructureSection load='1bds' size='340' side='right'caption='[[1bds]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1bds]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | </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> | ||
<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> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Anemonia sulcata]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Clore | [[Category: Clore GM]] | ||
[[Category: Driscoll | [[Category: Driscoll PC]] | ||
[[Category: Gronenborn | [[Category: Gronenborn AM]] | ||
Revision as of 12:54, 19 April 2023
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
FunctionBDS1_ANESU Blocks specifically the Kv3.4/KCNC4 potassium channel. Reduces blood pressure.[1] Publication Abstract from PubMedThe 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
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