Gould R J, Polokoff M A, Friedman P A, Huang T F, Holt J C, Cook J J, Niewiarowski S
Department of Biological Chemistry, Merck, Sharp & Dohme Research Laboratories, West Point, Pennsylvania 19486.
Proc Soc Exp Biol Med. 1990 Nov;195(2):168-71. doi: 10.3181/00379727-195-43129b.
Disintegrins represent a new class of low molecular weight, RGD-containing, cysteine-rich peptides isolated from the venom of various snakes. They interact with the beta 1 and beta 3 families of integrins and their potency is at least 500-2000 times higher than short RGDX peptides. Analysis of the amino acid sequences of 14 different disintegrins suggests that the RGD sequence, in the spatial configuration determined by the appropriate pairing of the cysteine residues, functions as a cell recognition site. However, certain nonconserved amino acids appear to modify the activity of disintegrins, their specificity for various receptors, and their ability to compete specifically with various ligands.
解整合素是一类新的低分子量、含RGD、富含半胱氨酸的肽，从多种蛇的毒液中分离得到。它们与整合素的β1和β3家族相互作用，其效力比短RGDX肽至少高500 - 2000倍。对14种不同解整合素的氨基酸序列分析表明，在由半胱氨酸残基适当配对所确定的空间构型中，RGD序列作为细胞识别位点发挥作用。然而，某些非保守氨基酸似乎会改变解整合素的活性、它们对各种受体的特异性以及它们与各种配体特异性竞争的能力。
