Structure and function of ameloblastin as an extracellular matrix protein: adhesion, calcium binding, and CD63 interaction in human and mouse.
Structure and function of ameloblastin as an extracellular matrix protein: adhesion, calcium binding, and CD63 interaction in human and mouse.
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DOI:
10.1111/j.1600-0722.2011.00889.x
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发表时间:
2011-12
影响因子:
1.9
通讯作者:
Luan X
中科院分区:
文献类型:
--
作者:
Zhang X;Diekwisch TG;Luan X
The functional significance of extracellular matrix proteins in the life of vertebrates is underscored by a high level of sequence variability in tandem with a substantial degree of conservation in terms of cell-cell and cell-matrix adhesion interactions. Many extracellular matrix proteins feature multiple adhesion domains for successful attachment to substrates, such as integrin, CD63, and heparin. Here we have used homology and ab initio modeling algorithms to compare mouse (mAMBN) and human ameloblastin (hABMN) isoforms and to analyze their potential for cell adhesion and interaction with other matrix molecules as well as calcium binding. Sequence comparison between mAMBN and hAMBN revealed a 26 amino acid deletion in mAMBN, corresponding to a helix-loop-helix frameshift. The human AMBN domain (174Q-201G) homologous to the mAMBN 157E-178I helix-loop-helix region formed a helix/loop motif with an extended loop, suggesting a higher degree of flexibility of the hAMBN compared to mAMBN, as confirmed by Molecular Dynamics simulation. Heparin binding domains, CD63 interaction domains, and calcium binding sites in both hAMBN and mAMBN support the concept of AMBN as an extracellular matrix protein. The high level of conservation between AMBN functional domains related to adhesion and differentiation was remarkable when compared to only 61% amino acid sequence homology.
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