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Self‐complementary motifs (SCM) in α‐crystallin small heat shock proteins
Author(s) -
Farnsworth Patricia N.,
Singh Kamalendra
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02051-2
Subject(s) - crystallin , chaperone (clinical) , protein subunit , heat shock protein , structural motif , chemistry , conserved sequence , homology modeling , homology (biology) , hsp70 , protein structure , biochemistry , protein domain , hydrogen bond , peptide sequence , amino acid , molecule , enzyme , medicine , pathology , gene , organic chemistry
Small heat shock proteins (sHsp) have been implicated in many cell processes involving the dynamics of protein–protein interactions. Two unusual sequences containing self‐complementary motifs (SCM) have been identified within the conserved α‐crystallin domain of sHsps. When two SCMs are aligned in an anti‐parallel direction (N to C and C to N), the charged or polar residues form either salt bridges or hydrogen bonds while the non‐polar residues participate in hydrophobic interactions. When aligned in reverse order, the residues of these motifs in α‐crystallin subunits form either hydrophobic and/or polar interactions. Homology based molecular modeling of the C‐terminal domain of α‐crystallin subunits using the crystal structure of MjHSP16.5 suggests that SCM1 and 2 participate in stabilizing secondary structure and subunit interactions. Also there is overwhelming evidence that these motifs are important in the chaperone‐like activity of α‐crystallin subunits. These sequences are conserved and appear to be characteristic of the entire sHsp superfamily. Similar motifs are also present in the Hsp70 family and the immunoglobulin superfamily.