期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 371, 期 3, 页码 717-724出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2007.05.054
关键词
crystal structure; C2 domain; lactadherin; factor V; factor VIII
资金
- NHLBI NIH HHS [R01 HL018834-29] Funding Source: Medline
Lactadherin, a glycoprotein secreted by a variety of cell types, contains two EGF domains and two C domains with sequence homology to the C domains of blood coagulation proteins factor V and factor VIII. Like these proteins, lactadherin binds to phosphatidylserine (PS)-containing membranes with high affinity. We determined the crystal structure of the bovine lactadherin C2 domain (residues 1 to 158) at 2.4 angstrom. The lactadherin C2 structure is similar to the C2 domains of factors V and VIII (rmsd of C-alpha atoms of 0.9 angstrom and 1.2 angstrom, and sequence identities of 43% and 38%, respectively). The lactadherin C2 domain has a discoidin-like fold containing two beta-sheets of five and three antiparallel beta-strands packed against one another. The N and C termini are linked by a disulfide bridge between Cys1 and Cys158. One beta-turn and two loops containing solvent-exposed hydrophobic residues extend from the C2 domain beta-sandwich core. In analogy with the C2 domains of factors V and VIII, some or all of these solvent-exposed hydrophobic residues, Trp26, Leu28, Phe31, and Phe81, likely participate in membrane binding. The C2 domain of lactadherin may serve as a marker of cell surface phosphatidylserine exposure and may have potential as a unique anti-thrombotic agent. (c) 2007 Elsevier Ltd. All rights reserved.
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