AMINO ACID RESIDUES WHICH CONFER [Greek small letter alpha]2 RECEPTOR SUBTYPE SPECIFICITY ARE LOCATED ON TRANSMEMBRANE DOMAINS IV - VI

1998 ◽  
Vol 89 (Supplement) ◽  
pp. 192A
Author(s):  
K. Takada ◽  
K. Harasawa ◽  
T. Kamibayashi ◽  
M. Maze
Keyword(s):  
Amino Acid ◽  
Transmembrane Domains ◽  
Receptor Subtype ◽  
Amino Acid Residues ◽  
Small Letter ◽  
Subtype Specificity

Comparison of the Amino Acid Residues in the Sixth Transmembrane Domains Accessible in the Binding-Site Crevices of μ, δ, and κ Opioid Receptors†

Biochemistry ◽  
2001 ◽  
Vol 40 (27) ◽  
pp. 8018-8029 ◽  
Author(s):  
Wei Xu ◽  
Jin Li ◽  
Chongguang Chen ◽  
Peng Huang ◽  
Harel Weinstein ◽  
...  
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Opioid Receptors ◽  
Transmembrane Domains ◽  
Amino Acid Residues

Structure of a Plasmodium yoelii gene-encoded protein homologous to the Ca(2+)-ATPase of rabbit skeletal muscle sarcoplasmic reticulum

1990 ◽  
Vol 97 (3) ◽  
pp. 487-495
Author(s):  
K. Murakami ◽  
K. Tanabe ◽  
S. Takada
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Amino Acid ◽  
Sarcoplasmic Reticulum ◽  
Amino Acid Sequence ◽  
Plasmodium Yoelii ◽  
Transmembrane Domains ◽  
Rabbit Skeletal Muscle ◽  
Parasite Development ◽  
Amino Acid Residues

A cation-transporting ATPase gene of Plasmodium yoelii was cloned from the parasite genomic library using an oligonucleotide probe derived from a conserved amino acid sequence of the phosphorylation domain of the aspartyl phosphate family of ATPases. The complete nucleotide sequence was determined and it predicts a 126,717 Mr encoded protein composed of 1115 amino acids. Northern blot analysis revealed that the gene is transcribed during the asexual stages of parasite development. The P. yoelii protein contains functional and structural features common to the family of aspartyl phosphate cation-transporting ATPases. The parasite protein shows the highest overall homology in amino acid sequence (42%) to the Ca2(+)-ATPase of rabbit skeletal muscle sarcoplasmic reticulum. Homologies to other aspartyl phosphate cation-transporting ATPases including a plasma membrane Ca2(+)-ATPase were between 13 and 24%. The structure predicted from a hydropathy plot also shows 10 transmembrane domains, the number and location of which correlated well with the sarcoplasmic reticulum Ca2(+)-ATPase. On the basis of these results, we conclude that the parasite gene encodes an organellar, but not plasma membrane, Ca2(+)-ATPase. The P. yoelii protein, furthermore, contains all six amino acid residues in the transmembrane domains that were recently identified as comprising a high-affinity Ca2(+)-binding site. It follows that organellar Ca2(+)-ATPases of rabbit and Plasmodium conserve functionally important amino acid residues, even though they are remote from each other phylogenetically.

Use of an in Situ Disulfide Cross-Linking Strategy To Map Proximities between Amino Acid Residues in Transmembrane Domains I and VII of the M3Muscarinic Acetylcholine Receptor

Biochemistry ◽  
2002 ◽  
Vol 41 (24) ◽  
pp. 7647-7658 ◽  
Author(s):  
Fadi F. Hamdan ◽  
Stuart D. C. Ward ◽  
Nasir A. Siddiqui ◽  
Lanh M. Bloodworth ◽  
Jürgen Wess
Keyword(s):  
Amino Acid ◽  
Acetylcholine Receptor ◽  
Transmembrane Domains ◽  
Cross Linking ◽  
Amino Acid Residues

Muscarinic Toxin-Like Proteins from Taiwan Banded Krait (Bungarus multicinctus) Venom: Purification, Characterization and Gene Organization

2002 ◽  
Vol 383 (9) ◽  
pp. 1397-1406 ◽  
Author(s):  
C. Chung ◽  
B.-N. Wu ◽  
C.-C. Yang ◽  
L.-S. Chang
Keyword(s):  
Amino Acid ◽  
Gene Organization ◽  
Receptor Subtype ◽  
Amino Acid Residues ◽  
Cd Spectra ◽  
Dna Encoding ◽  
Novel Proteins ◽  
Acrylamide Quenching ◽  
Venom Proteins ◽  
Quinuclidinyl Benzilate

Abstract Two novel proteins, BM8 and BM14, were isolated from Bungarus multicinctus (Taiwan banded krait) venom using the combination of chromatography on a SPSephadex C-25 column and a reversephase HPLC column. Both proteins contained 82 amino acid residues including 10 cysteine residues, but there were two amino acid substitutions at positions 37 and 38 (Glu37Ala38 in BM8; Lys37Lys38 in BM14). CD spectra and acrylamide quenching studies revealed that the gross conformation of BM8 and BM14 differed. In contrast to BM8, BM14 inhibited the binding of [3H]quinuclidinyl benzilate to the M2 muscarinic acetylcholine (mAchR) receptor subtype. Trinitrophenylation of Lys residues abolished the mAchRbinding activity of BM14, indicating that the Lys substitutions at positions 37 and 38 played a crucial role in the activity of BM14. The genomic DNA encoding the precursor of BM14 was amplified by PCR. The gene shared virtually identical structural organization with αneurotoxin and cardiotoxin genes. The intron sequences of these genes shared a sequence identity up to 84%, but the proteincoding regions were highly variable. These results suggest that BM8, BM14, neurotoxins and cardiotoxins may have originated from a common ancestor, and the evolution of snake venom proteins shows a tendency to diversify their functions.

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