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Volumn 98, Issue 24, 2001, Pages 13519-13524
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The 2.0-Å crystal structure of tachylectin 5A provides evidence for the common origin of the innate immunity and the blood coagulation systems
a
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Author keywords
[No Author keywords available]
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Indexed keywords
COAGULOGEN;
FIBRINOGEN;
LECTIN;
PROTEIN;
TACHYLECTIN 5A;
UNCLASSIFIED DRUG;
LIGAND;
PLASMA PROTEIN;
TL 5A PROTEIN, TACHYPLEUS TRIDENTATUS;
TL-5A PROTEIN, TACHYPLEUS TRIDENTATUS;
ARTHROPOD;
ARTICLE;
BLOOD CLOTTING;
CRYSTAL STRUCTURE;
EVOLUTION;
HEMOLYMPH;
HEMOSTASIS;
HOST RESISTANCE;
IMMUNITY;
INVERTEBRATE;
LIMULUS;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN FOLDING;
AMINO ACID SEQUENCE;
ANIMAL;
CHEMICAL STRUCTURE;
CHEMISTRY;
HUMAN;
IMMUNOLOGY;
INNATE IMMUNITY;
MOLECULAR EVOLUTION;
MOLECULAR GENETICS;
PHYSIOLOGY;
PROTEIN BINDING;
PROTEIN TERTIARY STRUCTURE;
SEQUENCE HOMOLOGY;
X RAY CRYSTALLOGRAPHY;
ARTHROPODA;
DECAPODA (CRUSTACEA);
INVERTEBRATA;
LIMULUS;
MAMMALIA;
MEROSTOMATA;
TACHYPLEUS TRIDENTATUS;
VERTEBRATA;
AMINO ACID SEQUENCE;
ANIMALS;
BLOOD COAGULATION;
BLOOD PROTEINS;
CRYSTALLOGRAPHY, X-RAY;
EVOLUTION, MOLECULAR;
FIBRINOGEN;
HORSESHOE CRABS;
HUMANS;
IMMUNITY, NATURAL;
LECTINS;
LIGANDS;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
PROTEIN BINDING;
PROTEIN FOLDING;
PROTEIN STRUCTURE, TERTIARY;
SEQUENCE HOMOLOGY, AMINO ACID;
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EID: 0035923237
PISSN: 00278424
EISSN: None
Source Type: Journal
DOI: 10.1073/pnas.201523798 Document Type: Article |
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Times cited : (126)
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References (31)
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