Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site - Wikidata - awgldk - TriplyDB

Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site

Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site

http://www.wikidata.org/entity/Q35037226

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Antigenic peptide trimming by ER aminopeptidases--insights from structural studies Binding structure of the leucine aminopeptidase inhibitor microginin FR1 Structural basis for the inhibition of the essential Plasmodium falciparum M1 neutral aminopeptidase Synthesis of New (−)-Bestatin-Based Inhibitor Libraries Reveals a Novel Binding Mode in the S1 Pocket of the Essential Malaria M1 Metalloaminopeptidase Structural basis for antigenic peptide precursor processing by the endoplasmic reticulum aminopeptidase ERAP1 Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming Structural Bases of Coronavirus Attachment to Host Aminopeptidase N and Its Inhibition by Neutralizing Antibodies The X-ray Crystal Structure of Human Aminopeptidase N Reveals a Novel Dimer and the Basis for Peptide Processing Structural basis for multifunctional roles of mammalian aminopeptidase N Discovery of α,β- and α,γ-diamino acid scaffolds for the inhibition of M1 family aminopeptidases A Novel Family of Soluble Minimal Scaffolds Provides Structural Insight into the Catalytic Domains of Integral Membrane Metallopeptidases A Naturally Variable Residue in the S1 Subsite of M1 Family Aminopeptidases Modulates Catalytic Properties and Promotes Functional Specialization Distribution and biochemical properties of an M1-family aminopeptidase in Plasmodium falciparum indicate a role in vacuolar hemoglobin catabolism An overview of heavy-atom derivatization of protein crystals The Plasmodium falciparum malaria M1 alanyl aminopeptidase (PfA-M1): insights of catalytic mechanism and function from MD simulations Characterization of a Vibrio fischeri aminopeptidase and evidence for its influence on an early stage of squid colonization Allosteric inhibition of aminopeptidase N functions related to tumor growth and virus infection.Aminopeptidase B, a glucagon-processing enzyme: site directed mutagenesis of the Zn2+-binding motif and molecular modelling CD13 is dispensable for normal hematopoiesis and myeloid cell functions in the mouse An integrated approach to the ligand binding specificity of Neisseria meningitidis M1 alanine aminopeptidase by fluorogenic substrate profiling, inhibitory studies and molecular modeling.Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.Identification and development of specific inhibitors for insulin-regulated aminopeptidase as a new class of cognitive enhancers.Structural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E. coli aminopeptidase N.Engagement of the S1, S1' and S2' subsites drives efficient catalysis of peptide bond hydrolysis by the M1-family aminopeptidase from Plasmodium falciparum.Intestinal peptidases form functional complexes with the neutral amino acid transporter B(0)AT1.Histidine 379 of human laeverin/aminopeptidase Q, a nonconserved residue within the exopeptidase motif, defines its distinctive enzymatic properties The gates of ion channels and enzymes.Architecture and function of metallopeptidase catalytic domains.Exploration of Sitagliptin as a potential inhibitor for the M1 Alanine aminopeptidase enzyme in Plasmodium falciparum using computational docking.Insight into the remarkable affinity and selectivity of the aminobenzosuberone scaffold for the M1 aminopeptidases family based on structure analysis.Biochemical characterization of aminopeptidase N2 from Toxoplasma gondii.Development of bestatin-based activity-based probes for metallo-aminopeptidases.Glu121-Lys319 salt bridge between catalytic and N-terminal domains is pivotal for the activity and stability of Escherichia coli aminopeptidase N.Crystal structure of leukotriene A4 hydrolase in complex with kelatorphan, implications for design of zinc metallopeptidase inhibitors.Combinatorial multicomponent access to natural-products-inspired peptidomimetics: discovery of selective inhibitors of microbial metallo-aminopeptidases.

P2860

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P2860

Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site

http://www.wikidata.org/entity/Q35037226

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2006 nî lūn-bûn

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2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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2006 թվականի օգոստոսին հրատարակված գիտական հոդված

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2006年の論文

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2006年学术文章

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Structure of aminopeptidase N ...... tmentalized, gated active site

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Structure of aminopeptidase N ...... tmentalized, gated active site

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Anthony Addlagatta

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P2860

Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation

Human aminopeptidase N is a receptor for human coronavirus 229E

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Coot: model-building tools for molecular graphics

Automated protein model building combined with iterative structure refinement

Main-chain bond lengths and bond angles in protein structures

SHELXL: high-resolution refinement

The CCP4 suite: programs for protein crystallography

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