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PubMed:16809340 JSONTXT 41 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
TextSentencer_T1 0-117 Sentence denotes Structural and computational characterization of the SHV-1 beta-lactamase-beta-lactamase inhibitor protein interface.
T1 0-117 Sentence denotes Structural and computational characterization of the SHV-1 beta-lactamase-beta-lactamase inhibitor protein interface.
TextSentencer_T2 118-254 Sentence denotes Beta-lactamase inhibitor protein (BLIP) binds a variety of class A beta-lactamases with affinities ranging from micromolar to picomolar.
T2 118-254 Sentence denotes Beta-lactamase inhibitor protein (BLIP) binds a variety of class A beta-lactamases with affinities ranging from micromolar to picomolar.
TextSentencer_T3 255-394 Sentence denotes Whereas the TEM-1 and SHV-1 beta-lactamases are almost structurally identical, BLIP binds TEM-1 approximately 1000-fold tighter than SHV-1.
T3 255-394 Sentence denotes Whereas the TEM-1 and SHV-1 beta-lactamases are almost structurally identical, BLIP binds TEM-1 approximately 1000-fold tighter than SHV-1.
TextSentencer_T4 395-606 Sentence denotes Determining the underlying source of this affinity difference is important for understanding the molecular basis of beta-lactamase inhibition and mechanisms of protein-protein interface specificity and affinity.
T4 395-606 Sentence denotes Determining the underlying source of this affinity difference is important for understanding the molecular basis of beta-lactamase inhibition and mechanisms of protein-protein interface specificity and affinity.
TextSentencer_T5 607-675 Sentence denotes Here we present the 1.6A resolution crystal structure of SHV-1.BLIP.
T5 607-675 Sentence denotes Here we present the 1.6A resolution crystal structure of SHV-1.BLIP.
TextSentencer_T6 676-803 Sentence denotes In addition, a point mutation was identified, SHV D104E, that increases SHV.BLIP binding affinity from micromolar to nanomolar.
T6 676-803 Sentence denotes In addition, a point mutation was identified, SHV D104E, that increases SHV.BLIP binding affinity from micromolar to nanomolar.
TextSentencer_T7 804-976 Sentence denotes Comparison of the SHV-1.BLIP structure with the published TEM-1.BLIP structure suggests that the increased volume of Glu-104 stabilizes a key binding loop in the interface.
T7 804-976 Sentence denotes Comparison of the SHV-1.BLIP structure with the published TEM-1.BLIP structure suggests that the increased volume of Glu-104 stabilizes a key binding loop in the interface.
TextSentencer_T8 977-1120 Sentence denotes Solution of the 1.8A SHV D104K.BLIP crystal structure identifies a novel conformation in which this binding loop is removed from the interface.
T8 977-1120 Sentence denotes Solution of the 1.8A SHV D104K.BLIP crystal structure identifies a novel conformation in which this binding loop is removed from the interface.
TextSentencer_T9 1121-1316 Sentence denotes Using these structural data, we evaluated the ability of EGAD, a program developed for computational protein design, to calculate changes in the stability of mutant beta-lactamase.BLIP complexes.
T9 1121-1316 Sentence denotes Using these structural data, we evaluated the ability of EGAD, a program developed for computational protein design, to calculate changes in the stability of mutant beta-lactamase.BLIP complexes.
TextSentencer_T10 1317-1547 Sentence denotes Changes in binding affinity were calculated within an error of 1.6 kcal/mol of the experimental values for 112 mutations at the TEM-1.BLIP interface and within an error of 2.2 kcal/mol for 24 mutations at the SHV-1.BLIP interface.
T10 1317-1547 Sentence denotes Changes in binding affinity were calculated within an error of 1.6 kcal/mol of the experimental values for 112 mutations at the TEM-1.BLIP interface and within an error of 2.2 kcal/mol for 24 mutations at the SHV-1.BLIP interface.
TextSentencer_T11 1548-1783 Sentence denotes The reasonable success of EGAD in predicting changes in interface stability is a promising step toward understanding the stability of the beta-lactamase.BLIP complexes and computationally assisted design of tight binding BLIP variants.
T11 1548-1783 Sentence denotes The reasonable success of EGAD in predicting changes in interface stability is a promising step toward understanding the stability of the beta-lactamase.BLIP complexes and computationally assisted design of tight binding BLIP variants.