Self‐complementary motifs (SCM) in α‐crystallin small heat shock proteins

FEBS Letters

Singh, Kamalendra²  Farnsworth, Patricia N.¹ 

[1] Department of Pharmacology and Physiology, UMD-New Jersey Medical School, 185 South Orange Ave., Newark, NJ 07103, USA;Department of Biochemistry and Molecular Biology, UMD-New Jersey Medical School, 185 South Orange Ave., Newark, NJ 07103, USA

关键词: Small heat shock protein;    α-Crystallin;    Chaperone activity;    Molecular modeling;    Amino acid sequence motif;   

DOI  :  10.1016/S0014-5793(00)02051-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown