Modulation of inhibitory activity of xylanase - α-amylase inhibitor protein (XAIP): Binding studies and crystal structure determination of XAIP- II from Scadoxus multiflorus at 1.2 Å resolution

BMC Structural Biology

Volumn 10, Issue , 2010, Pages

  Kumar, Sanjit ^a   Singh, Nagendra ^a   Mishra, Biswajit ^a   Dube, Divya ^a   Sinha, Mau ^a   Singh, S Baskar ^a   Dey, Sharmistha ^a   Kaur, Punit ^a   Sharma, Sujata ^a   Singh, Tej P ^a  

^a ALL INDIA INSTITUTE OF MEDICAL SCIENCES   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMYLASE GH13; ENZYME; INHIBITOR PROTEIN; UNCLASSIFIED DRUG; XYLANASE ALPHA AMYLASE INHIBITOR PROTEIN; XYLANASE ALPHA AMYLASE INHIBITOR PROTEIN II; XYLANASE GH11; AMYLASE; ENDO 1,4 BETA XYLANASE; ENZYME INHIBITOR; ISOPROTEIN; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CONFORMATION; CONTROLLED STUDY; CORRELATION ANALYSIS; CRYSTAL STRUCTURE; ENZYME INHIBITION; MODULATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PLANT; PLANT BULB; PROTEIN BINDING; PROTEIN INTERACTION; SCADOXUS MULTIFLORUS; AMINO ACID SUBSTITUTION; ANGIOSPERM; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; DRUG ANTAGONISM; ENZYMOLOGY; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION; SURFACE PLASMON RESONANCE; X RAY CRYSTALLOGRAPHY;

SCADOXUS MULTIFLORUS;

ALPHA-AMYLASES; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BASE SEQUENCE; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ENDO-1,4-BETA XYLANASES; ENZYME INHIBITORS; LILIACEAE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLANT PROTEINS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, QUATERNARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; SURFACE PLASMON RESONANCE;

EID: 78349303041     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-10-41     Document Type: Article

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