The large non-collagenous domain (NC-1) of type VII collagen is amino-terminal and chimeric. Homology to cartilage matrix protein, the type III domains of fibronectin and the A domains of von Willebrand factor.
The large non-collagenous domain (NC-1) of type VII collagen is amino-terminal and chimeric. Homology to cartilage matrix protein, the type III domains of fibronectin and the A domains of von Willebrand factor.
复制标题
VII 型胶原蛋白的大非胶原结构域 (NC-1) 是氨基末端且嵌合的。
DOI：
10.1093/hmg/1.7.475
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发表时间：
1992
影响因子：
3.5
通讯作者：
Uitto,J
中科院分区：
文献类型：
--
作者：
Christiano,AM;Rosenbaum,LM;Chung-Honet,LC;Parente,MG;Woodley,DT;Pan,TC;Zhang,RZ;Chu,ML;Burgeson,RE;Uitto,J
VII型胶原是锚定原纤维的主要成分，由两侧为非胶原结构域NC-1和NC-2的中央胶原三螺旋段组成。在这项研究中，我们研究了域组织的人VII型胶原蛋白通过分析推导的氨基酸序列来自克隆互补和基因组DNA，相比，来自羊膜VII型胶原蛋白的肽段。结果表明，来自VII型胶原NC-1结构域的肽段可归属于复合cDNA的5′端，表明NC-1位于分子的氨基末端。在NC-1中还鉴定了与粘附分子具有同源性的几个亚结构域。这些蛋白质结构域可以赋予NC-1粘附特性，从而促进VII型胶原与皮肤基底膜中的致密层和真皮内的锚定斑块的结合。
Type VII collagen, the major component of anchoring fibrils, consists of a central collagenous triple-helical segment flanked by non-collagenous domains, NC-1 and NC-2. In this study, we examined the domain organization of human type VII collagen through analysis of deduced amino acid sequences derived from cloned complementary and genomic DNAs, as compared to peptide segments derived from amniotic membrane type VII collagen. The results revealed that the peptide segments derived from the NC-1 domain of type VII collagen could be assigned to the 5′ portion of the composite cDNA, indicating that NC-1 resides at the amino terminal end of the molecule. Several sub-domains with homology to adhesive molecules were also identified within NC-1. These protein domains may confer adhesive properties to NC-1, thereby facilitating the binding of type VII collagen to the lamina densa in the cutaneous basement membrane and the anchoring plaques within the dermis.