1jc6

From Proteopedia

(Difference between revisions)

Revision as of 16:26, 10 September 2015

SOLUTION STRUCTURE OF BUNGARUS FACIATUS IX, A KUNITZ-TYPE CHYMOTRYPSIN INHIBITOR

Structural highlights

1jc6 is a 1 chain structure with sequence from Bungarus fasciatus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[VKT9_BUNFA] Dual-function toxin that inhibits both serine proteases (high activity on chymotrypsin (Ki = 18 nM), and low activity on elastase) and voltage-gated potassium channels Kv1.3/KCNA3 (IC(50) = 120.0 nM).^[1] ^[2]

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

Bungarus fasciatus fraction IX (BF9), a chymotrypsin inhibitor, consists of 65 amino acid residues with three disulfide bridges. It was isolated from the snake venom of B. fasciatus by ion-exchange chromatography and belongs to the bovine pancreatic trypsin inhibitor (BPTI)-like superfamily. It showed a dissociation constant of 5.8 x 10(-8) m with alpha-chymotrypsin as measured by a BIAcore binding assay system. The isothermal titration calorimetry revealed a 1:1 binding stoichiometry between this inhibitor and chymotrypsin and apparently no binding with trypsin. We further used CD and NMR to determine the solution structure of this venom-derived chymotrypsin inhibitor. The three-dimensional NMR solution structures of BF9 were determined on the basis of 582 restraints by simulated annealing and energy minimization calculations. The final set of 10 NMR structures was well defined, with average root mean square deviations of 0.47 A for the backbone atoms in the secondary structure regions and 0.86 A for residues The side chains of Phe(23), Tyr(24), Tyr(25), Phe(35), and Phe(47) exhibited many long-range nuclear Overhauser effects and were the principal components of the hydrophobic core in BF9. To gain insight into the structure-function relationships among proteins in the BPTI-like superfamily, we compared the three-dimensional structure of BF9 with three BPTI-like proteins that possess distinct biological functions. These proteins possessed similar secondary structure elements, but the loop regions and beta-turn were different from one another. Based on residues at the functional site of each protein, we suggest that the flexibility, rigidity, and variations of the amino acid residues in both the loop and beta-turn regions are related to their biological functions.

Solution structure of a Kunitz-type chymotrypsin inhibitor isolated from the elapid snake Bungarus fasciatus.,Chen C, Hsu CH, Su NY, Lin YC, Chiou SH, Wu SH J Biol Chem. 2001 Nov 30;276(48):45079-87. Epub 2001 Sep 18. PMID:11562364^[3]

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

References

↑ Chen C, Hsu CH, Su NY, Lin YC, Chiou SH, Wu SH. Solution structure of a Kunitz-type chymotrypsin inhibitor isolated from the elapid snake Bungarus fasciatus. J Biol Chem. 2001 Nov 30;276(48):45079-87. Epub 2001 Sep 18. PMID:11562364 doi:10.1074/jbc.M106182200
↑ Yang W, Feng J, Wang B, Cao Z, Li W, Wu Y, Chen Z. BF9, the first functionally characterized snake toxin peptide with Kunitz-type protease and potassium channel inhibiting properties. J Biochem Mol Toxicol. 2014 Feb;28(2):76-83. doi: 10.1002/jbt.21538. Epub 2013, Nov 14. PMID:24243656 doi:http://dx.doi.org/10.1002/jbt.21538
↑ Chen C, Hsu CH, Su NY, Lin YC, Chiou SH, Wu SH. Solution structure of a Kunitz-type chymotrypsin inhibitor isolated from the elapid snake Bungarus fasciatus. J Biol Chem. 2001 Nov 30;276(48):45079-87. Epub 2001 Sep 18. PMID:11562364 doi:10.1074/jbc.M106182200

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/1jc6"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1jc6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bungarus_fasciatus Bungarus fasciatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JC6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JC6 FirstGlance]. <br>
-</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=1jc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jc6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jc6 RCSB], [http://www.ebi.ac.uk/pdbsum/1jc6 PDBsum]</span></td></tr>
+</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=1jc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jc6 OCA], [http://pdbe.org/1jc6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jc6 RCSB], [http://www.ebi.ac.uk/pdbsum/1jc6 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/IVB1_BUNFA IVB1_BUNFA]] Dual-function toxin that inhibits both serine proteases (high activity on chymotrypsin (Ki = 18 nM), and low activity on elastase) and voltage-gated potassium channels Kv1.3/KCNA3 (IC(50) = 120.0 nM).<ref>PMID:24243656</ref> <ref>PMID:11562364</ref>
+[[http://www.uniprot.org/uniprot/VKT9_BUNFA VKT9_BUNFA]] Dual-function toxin that inhibits both serine proteases (high activity on chymotrypsin (Ki = 18 nM), and low activity on elastase) and voltage-gated potassium channels Kv1.3/KCNA3 (IC(50) = 120.0 nM).<ref>PMID:11562364</ref> <ref>PMID:24243656</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 25: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1jc6" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1jc6

From Proteopedia

Revision as of 16:26, 10 September 2015

SOLUTION STRUCTURE OF BUNGARUS FACIATUS IX, A KUNITZ-TYPE CHYMOTRYPSIN INHIBITOR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox