3odv
X-ray structure of kaliotoxin by racemic protein crystallographyX-ray structure of kaliotoxin by racemic protein crystallography
Structural highlights
FunctionKAX31_ANDMA Potent inhibitor of large conductance calcium-activated potassium channels (BK-Ca). Also binds to the dendrotoxin sensitive voltage-dependent potassium channel. It appears to block channel activity by a simple bimolecular inhibition process. Induces a transient period of fast flickering in the channel openings, followed by an almost complete blockade of the channel. Its binding affinity to rat brain synaptosomes is 5-fold higher than this of KTX-3. Binding of the toxin to the channel is associated with significant structural rearrangements in both molecules. Publication Abstract from PubMedHere we report the total synthesis of kaliotoxin by 'one pot' native chemical ligation of three synthetic peptides. A racemic mixture of d- and l-kaliotoxin synthetic protein molecules gave crystals in the centrosymmetric space group P1[combining macron] that diffracted to atomic-resolution (0.95 A), enabling the X-ray structure of kaliotoxin to be determined by direct methods. Total chemical synthesis and X-ray structure of kaliotoxin by racemic protein crystallography.,Pentelute BL, Mandal K, Gates ZP, Sawaya MR, Yeates TO, Kent SB Chem Commun (Camb). 2010 Sep 28. PMID:20877851[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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