Solution Structure of a Kunitz-type Chymotrypsin Inhibitor Isolated from the Elapid Snake Bungarus fasciatus

Chen, Chinpan; Hsu, Chun‐Hua; Su, Ning-Yuan; Lin, Yu‐Ching; Chiou, Shyh‐Horng; Wu, Shih‐Hsiung

doi:10.1074/jbc.m106182200

Cited by 59 publications

(50 citation statements)

References 36 publications

(41 reference statements)

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“…They exhibit diverse functions for inhibiting serine proteinase enzymes. This superfamily is classified into two families based on protein structure; small Kunitz-type inhibitors and BPTI-like toxins and soft tick anticoagulant proteins [5]. The Kunitz BPTI proteinase inhibitor family is divisible into subgroups according to source and bioactivity.…”

Section: Introductionmentioning

confidence: 99%

Purification, characterization and molecular cloning of chymotrypsin inhibitor peptides from the venom of Burmese Daboia russelii siamensis

Guo

McClean²,

Shaw

et al. 2013

Peptides

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Section: Introductionmentioning

confidence: 99%

Purification, characterization and molecular cloning of chymotrypsin inhibitor peptides from the venom of Burmese Daboia russelii siamensis

Guo

McClean²,

Shaw

et al. 2013

Peptides

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“…BF9 contains 65 amino acids with three disulfide bonds and was shown to consist of a double-stranded antiparallel β-sheet and one α-helix. Cys14 of BPTI is adjacent to the P1 position, Lys15, and forms a disulfide bond with Cys38, while the corresponding P1 position in BF9 is Asn17 and the corresponding disulfide bond is Cys16-Cys40 based on sequence alignment of BPTI and BF9 [5]. Due to isomerization of the Cys14-Cys38 disulfide bond, two conformational isomers with different chirality were observed in BPTI in the NMR spectra [9,10].…”

Section: Introductionmentioning

confidence: 99%

“…The three-dimensional structure of one chymotrypsin inhibitor, BF9, from the Elapid snake Bungarus fasciatus has been reported [5]. BF9 contains 65 amino acids with three disulfide bonds and was shown to consist of a double-stranded antiparallel β-sheet and one α-helix.…”

Section: Introductionmentioning

confidence: 99%

“…This chymotrypsin inhibitor belongs to the class of non-neurotoxic snake Kunitz/BPTI inhibitors [1], which are different from their snake Kunitz/BPTI neurotoxic homologues, such as dendrotoxins, calcicludine and the B chain of β-bungarotoxin which act as Ca 2+ or K + channel blockers [2]. A comparative analysis of the Kunitz/BPTI inhibitors and their neurotoxic homologues indicated that residue changes in the active sites result in both conformational adjustment and functional divergence [3][4][5]. The Kunitz domain recognizes one or more proteases through a set of 10-14 residues that are located mainly in the primary binding loop and partly in the second loop [6].…”

Section: Introductionmentioning

confidence: 99%

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NMR Solution Structure of a Chymotrypsin Inhibitor from the Taiwan Cobra Naja naja atra

et al. 2013

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Abstract:The Taiwan cobra (Naja naja atra) chymotrypsin inhibitor (NACI) consists of 57 amino acids and is related to other Kunitz-type inhibitors such as bovine pancreatic trypsin inhibitor (BPTI) and Bungarus fasciatus fraction IX (BF9), another chymotrypsin inhibitor. Here we present the solution structure of NACI. We determined the NMR structure of NACI with a root-mean-square deviation of 0.37 Å for the backbone atoms and 0.73 Å for the heavy atoms on the basis of 1,075 upper distance limits derived from NOE peaks measured in its NOESY spectra. To investigate the structural characteristics of NACI, we compared the three-dimensional structure of NACI with BPTI and BF9. The structure of the NACI protein comprises one 3 10 -helix, one α-helix and one double-stranded antiparallel β-sheet, which is comparable with the secondary structures in BPTI and BF9. The RMSD value between the mean structures is 1.09 Å between NACI and BPTI and 1.27 Å between NACI and BF9. In addition to similar secondary and tertiary structure, NACI OPEN ACCESSMolecules 2013, 18 8907 might possess similar types of protein conformational fluctuations as reported in BPTI, such as Cys14-Cys38 disulfide bond isomerization, based on line broadening of resonances from residues which are mainly confined to a region around the Cys14-Cys38 disulfide bond.

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“…For example, cone snails have peptides that act as calcium or sodium channel blockers or bind to the nicotinic acetylcholine receptor (Nielsen et al, 2000). Small proteins or peptides found in snake venoms include the PLA 2 phospholipases (Kwong et al, 1989) and Kunitz-type serine protease inhibitors, such as the venom basic protease inhibitor (Chen et al, 2001) and the textilinins (Masci et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray analysis of a Kunitz-type inhibitor, textilinin-1 fromPseudonaja textilis textilis

et al. 2006

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Textilinin-1 (Txln-1), a Kunitz-type serine protease inhibitor, is a 59-amino-acid polypeptide isolated from the venom of the Australian Common Brown snake Pseudonaja textilis textilis. This molecule has been suggested as an alternative to aprotinin, also a Kunitz-type serine protease inhibitor, for use as an antibleeding agent in surgical procedures. Txln-1 shares only 47% amino-acid identity to aprotinin; however, six cysteine residues in the two peptides are in conserved locations. It is therefore expected that the overall fold of these molecules is similar but that they have contrasting surface features. Here, the crystallization of recombinant textilinin-1 (rTxln-1) as the free molecule and in complex with bovine trypsin (229 amino acids) is reported. Two organic solvents, phenol and 1,4-butanediol, were used as additives to facilitate the crystallization of free rTxln-1. Crystals of the rTxln-1-bovine trypsin complex diffracted to 2.0 Å resolution, while crystals of free rTxln-1 diffracted to 1.63 Å resolution.

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Solution Structure of a Kunitz-type Chymotrypsin Inhibitor Isolated from the Elapid Snake Bungarus fasciatus

Cited by 59 publications

References 36 publications

Purification, characterization and molecular cloning of chymotrypsin inhibitor peptides from the venom of Burmese Daboia russelii siamensis

Purification, characterization and molecular cloning of chymotrypsin inhibitor peptides from the venom of Burmese Daboia russelii siamensis

NMR Solution Structure of a Chymotrypsin Inhibitor from the Taiwan Cobra Naja naja atra

Crystallization and preliminary X-ray analysis of a Kunitz-type inhibitor, textilinin-1 fromPseudonaja textilis textilis

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