期刊
SCIENCE
卷 296, 期 5571, 页码 1308-1313出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1071559
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资金
- NIGMS NIH HHS [R01 GM52717, R01 GM062270] Funding Source: Medline
- NCPDCID CDC HHS [NCI-P30-CA-08784] Funding Source: Medline
Cadherins are transmembrane proteins that mediate adhesion between cells in the solid tissues of animals. Here we present the 3.1 angstrom resolution crystal structure of the whole, functional extracellular domain from C-cadherin, a representative classical cadherin. The structure suggests a molecular mechanism for adhesion between cells by classical cadherins, and it provides a new framework for understanding both cis (same cell) and trans (juxtaposed cell) cadherin interactions. The trans adhesive interface is a twofold symmetric interaction defined by a conserved tryptophan side chain at the membrane-distal end of a cadherin molecule from one cell, which inserts into a hydrophobic pocket at the membrane-distal end of a cadherin molecule from the opposing cell.
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