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Crystal Structure of Canine Milk Lysozyme Stabilized against Non-enzymatic DeamidationCrystal Structure of Canine Milk Lysozyme Stabilized against Non-enzymatic Deamidation
Structural highlights
FunctionLYSC1_CANLF Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.[PROSITE-ProRule:PRU00680] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAsparaginyl deamidation is a common form of nonenzymatic degradation of proteins and peptides. As it introduces a negative charge spontaneously and irreversibly, charge heterogeneity can be accumulated in protein solution during purification, preservation, and experiments. In this study, canine milk lysozyme (CML), a useful model for the study of the molten globule state, exhibited charge heterogeneity after sample purification. Four Asn residues in CML deamidated rapidly under mild conditions: pH 8.0 and 30 degrees C. Other than these residues, one Asn residue, which was stable in the native state, was labile to deamidation in the unfolded state. This suggests that the structural formation around Asn can suppress deamidation. Substitutions of these labile Asn residues to Gln residues prevented deamidation effectively. Because the substitutions did not disrupt the structural formation of the native and molten globule states, they will enable more precise analyses for physical and structural studies. Proteins 2008. (c) 2008 Wiley-Liss, Inc. Spontaneous asparaginyl deamidation of canine milk lysozyme under mild conditions.,Nonaka Y, Aizawa T, Akieda D, Yasui M, Watanabe M, Watanabe N, Tanaka I, Kamiya M, Mizuguchi M, Demura M, Kawano K Proteins. 2008 Jan 23;72(1):313-322. PMID:18214981[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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