Abstract
Members of the NTR/TNFR family mediate apoptosis in many tissues, yet sequence homology has not been detected in their intracellular domains except for a 'death domain' in TNFR-I and Fas. Here, a region of the 75 kDa neurotrophin receptor (NTR) has been aligned with this apoptosis-inducing motif. Peptides at the carboxyl terminus of each domain potentially form amphiphilic helices, one of which (in NTR) resembles mastoparan, a G-protein activating peptide. Molecular models of three death-region peptides suggest that observed sequence similarities reflect a common structure, perhaps capable of undergoing an induced coil to helix transition.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Antigens, CD / chemistry*
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Apoptosis*
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Humans
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Intercellular Signaling Peptides and Proteins
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Molecular Sequence Data
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Peptides
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Protein Structure, Secondary
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Receptor, Nerve Growth Factor
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Receptors, Neuropeptide / chemistry*
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Receptors, Tumor Necrosis Factor / chemistry*
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Receptors, Tumor Necrosis Factor, Type I
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Sequence Homology, Amino Acid
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Wasp Venoms / chemistry
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fas Receptor / chemistry
Substances
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Antigens, CD
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Intercellular Signaling Peptides and Proteins
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Peptides
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Receptor, Nerve Growth Factor
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Receptors, Neuropeptide
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Receptors, Tumor Necrosis Factor
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Receptors, Tumor Necrosis Factor, Type I
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Wasp Venoms
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fas Receptor
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mastoparan