4ttm

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(Difference between revisions)

Revision as of 06:45, 26 July 2016

Racemic structure of kalata B1 (kB1)

Structural highlights

4ttm is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	, , , , , , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KAB1_OLDAF] Probably participates in a plant defense mechanism. Has antibiotic activity. Has a diuretic effect. Has a uterotonic effect in humans. Active against the Gram-positive S.aureus with a minimum inhibition concentration of approximately 0.2 microM. Relatively ineffective against Gram-negative bacteria such as E.coli and P.aeruginosa. Inhibitory effect on the growth and development of larvae from H.punctigera. The unmodified form has hemolytic activity, the oxidized form lacks hemolytic activity. If the protein is linearized, hemolytic activity is lost.^[1] ^[2]

Publication Abstract from PubMed

Cyclic disulfide-rich peptides have exceptional stability and are promising frameworks for drug design. We were interested in obtaining X-ray structures of these peptides to assist in drug design applications, but disulfide-rich peptides can be notoriously difficult to crystallize. To overcome this limitation, we chemically synthesized the L- and D-forms of three prototypic cyclic disulfide-rich peptides: SFTI-1 (14-mer with one disulfide bond), cVc1.1 (22-mer with two disulfide bonds), and kB1 (29-mer with three disulfide bonds) for racemic crystallization studies. Facile crystal formation occurred from a racemic mixture of each peptide, giving structures solved at resolutions from 1.25 A to 1.9 A. Additionally, we obtained the quasi-racemic structures of two mutants of kB1, [G6A]kB1, and [V25A]kB1, which were solved at a resolution of 1.25 A and 2.3 A, respectively. The racemic crystallography approach appears to have broad utility in the structural biology of cyclic peptides.

Racemic and Quasi-Racemic X-ray Structures of Cyclic Disulfide-Rich Peptide Drug Scaffolds.,Wang CK, King GJ, Northfield SE, Ojeda PG, Craik DJ Angew Chem Int Ed Engl. 2014 Aug 28. doi: 10.1002/anie.201406563. PMID:25168664^[3]

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

References

↑ Plan MR, Goransson U, Clark RJ, Daly NL, Colgrave ML, Craik DJ. The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides. Chembiochem. 2007 Jun 18;8(9):1001-11. PMID:17534989 doi:http://dx.doi.org/10.1002/cbic.200700097
↑ Barry DG, Daly NL, Clark RJ, Sando L, Craik DJ. Linearization of a naturally occurring circular protein maintains structure but eliminates hemolytic activity. Biochemistry. 2003 Jun 10;42(22):6688-95. PMID:12779323 doi:http://dx.doi.org/10.1021/bi027323n
↑ Wang CK, King GJ, Northfield SE, Ojeda PG, Craik DJ. Racemic and Quasi-Racemic X-ray Structures of Cyclic Disulfide-Rich Peptide Drug Scaffolds. Angew Chem Int Ed Engl. 2014 Aug 28. doi: 10.1002/anie.201406563. PMID:25168664 doi:http://dx.doi.org/10.1002/anie.201406563

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/4ttm"

@@ Line 1: / Line 1: @@
 ==Racemic structure of kalata B1 (kB1)==
 <StructureSection load='4ttm' size='340' side='right' caption='[[4ttm]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4ttm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TTM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TTM FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAR:D-ARGININE'>DAR</scene>, <scene name='pdbligand=DCY:D-CYSTEINE'>DCY</scene>, <scene name='pdbligand=DGL:D-GLUTAMIC+ACID'>DGL</scene>, <scene name='pdbligand=DLE:D-LEUCINE'>DLE</scene>, <scene name='pdbligand=DPR:D-PROLINE'>DPR</scene>, <scene name='pdbligand=DSG:D-ASPARAGINE'>DSG</scene>, <scene name='pdbligand=DSN:D-SERINE'>DSN</scene>, <scene name='pdbligand=DTH:D-THREONINE'>DTH</scene>, <scene name='pdbligand=DTR:D-TRYPTOPHAN'>DTR</scene>, <scene name='pdbligand=DVA:D-VALINE'>DVA</scene></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=4ttm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ttm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ttm RCSB], [http://www.ebi.ac.uk/pdbsum/4ttm 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=4ttm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ttm OCA], [http://pdbe.org/4ttm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ttm RCSB], [http://www.ebi.ac.uk/pdbsum/4ttm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ttm ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4ttm" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4ttm

From Proteopedia

Revision as of 06:45, 26 July 2016

Racemic structure of kalata B1 (kB1)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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