Amino acids Conserved

One might expect these positions to exhibit a higher degree of amino acid conservation and hence sequence homology than the rest of the molecule. This is not, however, the case for distantly related molecules that have low sequence homology and derive from distantly related species. The sequence identity of these residues is no greater than in the rest of the... 

Immuno-histochemical staining of intracellular bacteria in filarial nematodes has been obtained using antibodies against GroELand catalase (Henkle-Duhrsen etal., 1998 Hoerauf etal., 1999) the specificity of these antibodies is unknown, but it is expected to be low because both GroEL and catalase show high level of amino acid conservation throughout the proteobacteria. nd = not done. 

Fig. 3. Alignment of poly(HA) depolymerase catalytic active amino acids. Amino acids of the catalytic triad and the conserved histidine residue of the putative oxyanion are shown in bold letters. The positions (pos.) of respective amino acids of mature depolymerase proteins are indicated. Amino acids conserved in all poly(HASCL) depolymerases are indicated in capital letters, those which have been conserved in ten or more proteins are marked by low letters in the consensus sequence. indicates amino acids with hydrophobic side chains + indicates amino acids with a small side chain...

Figure 2.20 Schematic representation of a zinc-finger domain from TFIIIA and related proteins. X represents any amino acid conserved amino acids are histidine (H), cysteine (C), tyrosine (Y), phenylalanine (F), and leucine (L).

Reversible protein phosphorylation occurs by means of protein kinases. Eukaryotic protein kinases comprise a 250-amino acid, conserved catalytic domain. They are widely exploited in the regulation of physiological processes according to estimates the mammalian genome contains over 2000 PK genes. 

Fig. 8.2 Alignment of the protein structure of the cysteinyl leukotriene 1 (CysLTj) and 2 (CysLT ) receptors in relation to rhodopsin. The amino acids conserved between these family A receptors are shown. The consensus is greater than 50%. These data formed the basis of the model predicting the CysLTj and CysLT transmembrane domains (helices 1-7), the four [3-sheets, and the putative cysteinyl leukotiiene-binding domain. The amino acid variants that are associated with atopy or asthma, the G300S CysLTj variant, and the M201V CysLT variant are each boxed and noted with arrows...

Figure 18.3 Alignment of moth ABPX and DmeIPBPRP proteins. Sources of the sequences and accession numbers are reported in Table 18.1. The amino acids conserved in ABPXs and DmelPBPRP-1 are represented in bold. Those amino acids found in DmelPBPRP-1 and ABPX or AipsABPX-1 and DmelPBPRP-1 are represented in italics. Conserved cysteines are underlined. These specific amino acids support the classification of these sequences as OBP1 type of proteins.

Models with five or six transmembrane helices for the a subunit have been proposed from combined interpretation of hydrophobicity estimation, amino acid conservation, and mutational analysis. As discussed in detail by Fillingame,6 the first three helices in the three models are similar, while one to three helices were proposed from different... 

Impressive amino-acid conservation was observed for recognition of the same nucleotide in different targets and the selected residues in many cases made good chemical sense (Fig. 10). For example, Asn in position 3 (Asn3) was virtually always selected to recognize adenine in the middle position, whether in the context of GAG, GAA, GAT, or GAC. Gln-1 and Arg-1 were always selected to recognize adenine or... 

Fig-i Structural considerations about drug binding in the Kvl.5 channel pore. Amino acid sequence comparison of alpha subunit sequences from human Kvl.1-1.6 and Kv2.1, Kvll.l (hERG), Kv7.1 (KvLQTl). Symbols indicate complete amino acid conservation ( ), conservative substitution among all aligned sequences ( ), and critical substitution in a generally conserved position (.)... 

In region 2, the loops on the N side of the /3-sheets (C end of the helices) have no amino acids conserved in all the sequences of the ADPGlc PPases... 

Fig. 3. Comparison of the amino-acid sequence of ribosomal protein L2 from eucarya (Ddi [112] and Spo [113]), archaea (Mva[109] and Hma[l 14]) and bacteria (Eco[115] and Bst[116]). See Table 2 for abbreviations. An asterisk, indicates amino acids conserved in all L2 proteins while a dot indicates...

FIGURE 2 Amino acid conservation between acetolactate synthase genes. The numbers indicate amino acid residues. The first bar represents a comparison of the deduced amino acid sequences of ALS from tobacco and Arabidopsis-, the second bar represents a comparison between the amino acid sequences of the three E. coli ALS isozymes. Regions of conservation are shown in white. 

Valdar, W.S., Thornton, J.M. Protein-protein interfaces Analysis of amino acid conservation in homodimers. Proteins 2001, 42(1), 108-24. 

Luscombe, N.M., Thornton, J.M. Protein-DNA interactions Amino acid conservation and the effects of mutations on binding specificity. J. Mol. Biol. 2002, 320, 991-1009. 

This primer was based on the urchin sequence. It is in a region of high amino acid conservation, but is not very useful for anything but sea urchins. 

Irving JA, Pike RN, Lesk AM et al. Phylogeny of the serpin superfamily Implications of patterns of amino acid conservation for structure and function. Genome Res 2000 10 1845-1864. 

Between core 2 and core 3 is a long stretch of amino acid sequence that contains few blocks of amino acid conservation and is variable in length among the peptide synthetase modules. Cosima et al. (55) have aligned the corresponding sequences from... 

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