2pqs
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(New page: 200px<br /><applet load="2pqs" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pqs, resolution 2.40Å" /> '''Crystal Structure of...)
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Revision as of 10:33, 23 January 2008
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Crystal Structure of the Bovine Lactadherin C2 Domain
Overview
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 A. The lactadherin, C2 structure is similar to the C2 domains of factors V and VIII (rmsd of, C(alpha) atoms of 0.9 A and 1.2 A, 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.
About this Structure
2PQS is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Crystal Structure of the Bovine Lactadherin C2 Domain, a Membrane Binding Motif, Shows Similarity to the C2 Domains of Factor V and Factor VIII., Lin L, Huai Q, Huang M, Furie B, Furie BC, J Mol Biol. 2007 Aug 17;371(3):717-24. Epub 2007 May 25. PMID:17583728
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