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Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus.

Standard

Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus. / García-Fernández, Rossana; Pons, Tirso; Meyer, Arne; Perbandt, Markus; González-González, Yamile; Gil, Dayrom; de Los Angeles Chávez, María; Betzel, Christian; Redecke, Lars.

in: ACTA CRYSTALLOGR F, Jahrgang 68, Nr. Pt 11, Pt 11, 2012, S. 1289-1293.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

García-Fernández, R, Pons, T, Meyer, A, Perbandt, M, González-González, Y, Gil, D, de Los Angeles Chávez, M, Betzel, C & Redecke, L 2012, 'Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus.', ACTA CRYSTALLOGR F, Jg. 68, Nr. Pt 11, Pt 11, S. 1289-1293. <http://www.ncbi.nlm.nih.gov/pubmed/23143234?dopt=Citation>

APA

García-Fernández, R., Pons, T., Meyer, A., Perbandt, M., González-González, Y., Gil, D., de Los Angeles Chávez, M., Betzel, C., & Redecke, L. (2012). Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus. ACTA CRYSTALLOGR F, 68(Pt 11), 1289-1293. [Pt 11]. http://www.ncbi.nlm.nih.gov/pubmed/23143234?dopt=Citation

Vancouver

García-Fernández R, Pons T, Meyer A, Perbandt M, González-González Y, Gil D et al. Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus. ACTA CRYSTALLOGR F. 2012;68(Pt 11):1289-1293. Pt 11.

Bibtex

@article{b02cc180554443e489fbbca65e587c68,
title = "Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus.",
abstract = "The BPTI/Kunitz-type inhibitor family includes several extremely potent serine protease inhibitors. To date, the inhibitory mechanisms have only been studied for mammalian inhibitors. Here, the first crystal structure of a BPTI/Kunitz-type inhibitor from a marine invertebrate (rShPI-1A) is reported to 2.5?{\AA} resolution. Crystallization of recombinant rShPI-1A required the salt-induced dissociation of a trypsin complex that was previously formed to avoid intrinsic inhibitor aggregates in solution. The rShPI-1A structure is similar to the NMR structure of the molecule purified from the natural source, but allowed the assignment of disulfide-bridge chiralities and the detection of an internal stabilizing water network. A structural comparison with other BPTI/Kunitz-type canonical inhibitors revealed unusual ? angles at positions 17 and 30 to be a particular characteristic of the family. A significant clustering of ? and ? angle values in the glycine-rich remote fragment near the secondary binding loop was additionally identified, but its impact on the specificity of rShPI-1A and similar molecules requires further study.",
keywords = "Animals, Amino Acid Sequence, Molecular Sequence Data, Models, Molecular, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Alignment, Crystallography, X-Ray, Recombinant Proteins/chemistry, Hydrogen Bonding, Conserved Sequence, *Sea Anemones, Structural Homology, Protein, Trypsin Inhibitor, Kunitz Soybean/*chemistry, Animals, Amino Acid Sequence, Molecular Sequence Data, Models, Molecular, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Alignment, Crystallography, X-Ray, Recombinant Proteins/chemistry, Hydrogen Bonding, Conserved Sequence, *Sea Anemones, Structural Homology, Protein, Trypsin Inhibitor, Kunitz Soybean/*chemistry",
author = "Rossana Garc{\'i}a-Fern{\'a}ndez and Tirso Pons and Arne Meyer and Markus Perbandt and Yamile Gonz{\'a}lez-Gonz{\'a}lez and Dayrom Gil and {de Los Angeles Ch{\'a}vez}, Mar{\'i}a and Christian Betzel and Lars Redecke",
year = "2012",
language = "English",
volume = "68",
pages = "1289--1293",
journal = "ACTA CRYSTALLOGR F",
issn = "2053-230X",
publisher = "John Wiley and Sons Ltd",
number = "Pt 11",

}

RIS

TY - JOUR

T1 - Structure of the recombinant BPTI/Kunitz-type inhibitor rShPI-1A from the marine invertebrate Stichodactyla helianthus.

AU - García-Fernández, Rossana

AU - Pons, Tirso

AU - Meyer, Arne

AU - Perbandt, Markus

AU - González-González, Yamile

AU - Gil, Dayrom

AU - de Los Angeles Chávez, María

AU - Betzel, Christian

AU - Redecke, Lars

PY - 2012

Y1 - 2012

N2 - The BPTI/Kunitz-type inhibitor family includes several extremely potent serine protease inhibitors. To date, the inhibitory mechanisms have only been studied for mammalian inhibitors. Here, the first crystal structure of a BPTI/Kunitz-type inhibitor from a marine invertebrate (rShPI-1A) is reported to 2.5?Å resolution. Crystallization of recombinant rShPI-1A required the salt-induced dissociation of a trypsin complex that was previously formed to avoid intrinsic inhibitor aggregates in solution. The rShPI-1A structure is similar to the NMR structure of the molecule purified from the natural source, but allowed the assignment of disulfide-bridge chiralities and the detection of an internal stabilizing water network. A structural comparison with other BPTI/Kunitz-type canonical inhibitors revealed unusual ? angles at positions 17 and 30 to be a particular characteristic of the family. A significant clustering of ? and ? angle values in the glycine-rich remote fragment near the secondary binding loop was additionally identified, but its impact on the specificity of rShPI-1A and similar molecules requires further study.

AB - The BPTI/Kunitz-type inhibitor family includes several extremely potent serine protease inhibitors. To date, the inhibitory mechanisms have only been studied for mammalian inhibitors. Here, the first crystal structure of a BPTI/Kunitz-type inhibitor from a marine invertebrate (rShPI-1A) is reported to 2.5?Å resolution. Crystallization of recombinant rShPI-1A required the salt-induced dissociation of a trypsin complex that was previously formed to avoid intrinsic inhibitor aggregates in solution. The rShPI-1A structure is similar to the NMR structure of the molecule purified from the natural source, but allowed the assignment of disulfide-bridge chiralities and the detection of an internal stabilizing water network. A structural comparison with other BPTI/Kunitz-type canonical inhibitors revealed unusual ? angles at positions 17 and 30 to be a particular characteristic of the family. A significant clustering of ? and ? angle values in the glycine-rich remote fragment near the secondary binding loop was additionally identified, but its impact on the specificity of rShPI-1A and similar molecules requires further study.

KW - Animals

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Models, Molecular

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

KW - Sequence Alignment

KW - Crystallography, X-Ray

KW - Recombinant Proteins/chemistry

KW - Hydrogen Bonding

KW - Conserved Sequence

KW - Sea Anemones

KW - Structural Homology, Protein

KW - Trypsin Inhibitor, Kunitz Soybean/chemistry

KW - Animals

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Models, Molecular

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

KW - Sequence Alignment

KW - Crystallography, X-Ray

KW - Recombinant Proteins/chemistry

KW - Hydrogen Bonding

KW - Conserved Sequence

KW - Sea Anemones

KW - Structural Homology, Protein

KW - Trypsin Inhibitor, Kunitz Soybean/chemistry

M3 - SCORING: Journal article

VL - 68

SP - 1289

EP - 1293

JO - ACTA CRYSTALLOGR F

JF - ACTA CRYSTALLOGR F

SN - 2053-230X

IS - Pt 11

M1 - Pt 11

ER -