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2pqs

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[[Image:2pqs.jpg|left|200px]]
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{{Structure
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|GENE= MFGE8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pqs OCA], [http://www.ebi.ac.uk/pdbsum/2pqs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pqs RCSB]</span>
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'''Crystal Structure of the Bovine Lactadherin C2 Domain'''
'''Crystal Structure of the Bovine Lactadherin C2 Domain'''
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[[Category: Furie, B C.]]
[[Category: Furie, B C.]]
[[Category: Huang, M.]]
[[Category: Huang, M.]]
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[[Category: c2 domain]]
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[[Category: C2 domain]]
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[[Category: cell adhesion]]
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[[Category: Cell adhesion]]
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[[Category: lactadherin]]
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[[Category: Lactadherin]]
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[[Category: membrane binding]]
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[[Category: Membrane binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:38:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:39:31 2008''
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Revision as of 10:38, 4 May 2008

Template:STRUCTURE 2pqs

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 Page seeded by OCA on Sun May 4 13:38:46 2008

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