2pqs
From Proteopedia
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- | [[Image:2pqs.jpg|left|200px]] | + | [[Image:2pqs.jpg|left|200px]] |
- | + | ||
- | '''Crystal Structure of the Bovine Lactadherin C2 Domain''' | + | {{Structure |
+ | |PDB= 2pqs |SIZE=350|CAPTION= <scene name='initialview01'>2pqs</scene>, resolution 2.40Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= MFGE8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure of the Bovine Lactadherin C2 Domain''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2PQS is a [ | + | 2PQS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQS OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17583728 17583728] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: membrane binding]] | [[Category: membrane binding]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:16:17 2008'' |
Revision as of 16:16, 20 March 2008
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, resolution 2.40Å | |||||||
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Gene: | MFGE8 (Bos taurus) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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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