Figure 5 of
Peterson, Mol Vis 2004;
10:857-866.Figure 5 of
Peterson, Mol Vis 2004;
10:857-866.
Figure 5. Primary sequence of bovine αA-crystallin and αB-crystallin
Tryptic cleavage residues are indicated by an asterisk under the amino acid. The approximate region of conserved α-crystallin domain is shown in capital letters for bovine αA-crystallin and αB-crystallin. Lysine residues that react with only one end of the bifunctional crosslinking reagent are shown in red and lysine residues that react with both ends of the bifunctional crosslinking reagent to form homo-oligomeric or hetero-oligomeric complexes are shown in blue. Note that αA-Lys11 and αA-Lys99 were found to be both modified and crosslinked and are shown in green. In αA-crystallin there are a total of 7 lysines and in αB-crystallin there are a total of 10 lysines.
αA-crystallin
Ac-mdiaiqhpwfkrtlgpfypsrlfdqffgeglfeydllpflsstispyyrq 50
** * *
slfrtvldsgisevrsdrdKFVIFLDVKHFSPEDLTVKVQEDFVEIHGKH 100
* * * * * * *
NERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKIPSGV 150
* * ** * *
DAGHSERAipvsreekpssapss 173
* * *
αB-crystallin
Ac-mdiaihhpwirrpffpfhspsrlfdqffgehllesdlfpastslspfylr 50
* *
ppsflrapswidtglsemrleKDRFSVNLDVKHFSPEELKVKVLGDVIEV 100
* * * * * *
HGKHEERQDEHGFISREFHRKYRIPADVDPLAITSSLSSDGVLTVNGPRK 150
* * *
QAsgpertipitreekpavtaapkk 175
* * * **
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