LOCALIZATION OF AN ARG-GLY-ASP RECOGNITION SITE WITHIN AN INTEGRIN ADHESION RECEPTOR
LOCALIZATION OF AN ARG-GLY-ASP RECOGNITION SITE WITHIN AN INTEGRIN ADHESION RECEPTOR
复制标题
DOI：
10.1126/science.3262922
复制
发表时间：
1988-10-07
期刊：
影响因子：
56.9
通讯作者：
PLOW, EF
中科院分区：
文献类型：
--
作者：
DSOUZA, SE;GINSBERG, MH;PLOW, EF
许多粘附相互作用由粘附蛋白中的Arg-Gly-Asp（RGD）序列介导。这种RGD序列经常被结构相关的异二聚体识别，所述异二聚体是粘附受体的整联蛋白家族的成员。在血小板RGD受体gpIIb/IIIa中发现了一个区域，RGD肽与该区域发生化学交联。该区域对应于gpIIIa的残基109至171。该片段在β-内酰胺酶中是保守的。亚基的整合素（76%的序列同一性），表明它可能发挥作用的粘附功能，这个家庭的受体。
Many adhesive interactions are mediated by Arg-Gly-Asp (RGD) sequences within adhesive proteins. Such RGD sequences are frequently recognized by structurally related heterodimers that are members of the integrin family of adhesion receptors. A region was found in the platelet RGD receptor, gpIIb/IIIa, to which an RGD peptide becomes chemically cross-linked. This region corresponds to residues 109 to 171 of gpIIIa. This segment is conserved among the .beta. subunits of the integrins (76 percent identity of sequence), indicating that it may play a role in the adhesive functions of this family of receptors.