Matsukura H, Michael A F, Fish A J, Butkowski R J
Department of Pediatrics, University of Minnesota, Minneapolis 55455.
Connect Tissue Res. 1992;28(3):231-44. doi: 10.3109/03008209209015039.
The globular domain (NC) of alpha 4(IV) collagen chain was partially sequenced and compared with the NC domain of other collagen IV chains. The alpha 4(IV) NC domain was found to be most closely related to alpha 2(IV) NC domain but distinct from the NC domain of alpha 1(IV), alpha 2(IV), alpha 3(IV) and alpha 5(IV) collagen chains. Partial sequence, representing nearly one half of alpha 4(IV) NC domain, shows 56%, 69%, 51% and 54% identity with the corresponding NC domains of alpha 1(IV), alpha 2(IV), alpha 3(IV) and alpha 5(IV) collagen chains, respectively. A short, highly polar, region of variable sequence is found near the carboxy terminus of alpha 4(IV) NC domain. This sequence corresponds to a non-conserved region among NC domains, suggesting functional specialization at this site. It exhibits high surface probability with predicted structural differences among NC domains. These results confirm uniqueness of alpha 4(IV) NC domain and indicate its structural relatedness to other NC domains of collagen IV.
对α4（IV）胶原链的球状结构域（NC）进行了部分测序，并与其他IV型胶原链的NC结构域进行了比较。发现α4（IV）NC结构域与α2（IV）NC结构域关系最为密切，但与α1（IV）、α2（IV）、α3（IV）和α5（IV）胶原链的NC结构域不同。代表α4（IV）NC结构域近一半的部分序列与α1（IV）、α2（IV）、α3（IV）和α5（IV）胶原链的相应NC结构域分别具有56%、69%、51%和54%的同一性。在α4（IV）NC结构域的羧基末端附近发现了一个短的、高度极性的可变序列区域。该序列对应于NC结构域之间的一个非保守区域，表明该位点具有功能特异性。它表现出高表面概率，且NC结构域之间存在预测的结构差异。这些结果证实了α4（IV）NC结构域的独特性，并表明其与IV型胶原其他NC结构域的结构相关性。
