3bn6

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of the C2 Domain of Bovine Lactadherin at 1.67 Angstrom Resolution

Structural highlights

3bn6 is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.67Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MFGM_BOVIN Contributes to phagocytic removal of apoptotic cells in many tissues. Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization (By similarity). Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Lactadherin is a phosphatidyl-L-serine (Ptd-L-Ser)-binding protein that decorates membranes of milk fat globules. The major Ptd-l-Ser binding function of lactadherin has been localized to its C2 domain, which shares homology with the C2 domains of blood coagulation factor VIII and factor V. Correlating with this homology, purified lactadherin competes efficiently with factors VIII and V for Ptd-L-Ser binding sites, functioning as a potent anticoagulant. We have determined the crystal structure of the lactadherin C2 domain (Lact-C2) at 1.7A resolution. The bovine Lact-C2 structure has a beta-barrel core that is homologous with the factor VIII C2 (fVIII-C2) and factor V C2 (fV-C2) domains. Two loops at the end of the beta-barrel, designated spikes 1 and 3, display four water-exposed hydrophobic amino acids, reminiscent of the membrane-interactive residues of fVIII-C2 and fV-C2. In contrast to the corresponding loops in fVIII-C2 and fV-C2, spike 1 of Lact-C2 adopts a hairpin turn in which the 7-residue loop is stabilized by internal hydrogen bonds. Further, central glycine residues in two membrane-interactive loops may enhance conformability of Lact-C2 to membrane binding sites. Mutagenesis studies confirmed a membrane-interactive role for the hydrophobic and/or Gly residues of both spike 1 and spike 3. Substitution of spike 1 of fVIII-C2 into Lact-C2 also diminished binding. Computational ligand docking studies identified two prospective Ptd-l-Ser interaction sites. These results identify two membrane-interactive loops of Lact-C2 and provide a structural basis for the more efficient phospholipid binding of lactadherin as compared with factor VIII and factor V.

Crystal structure of lactadherin C2 domain at 1.7A resolution with mutational and computational analyses of its membrane-binding motif.,Shao C, Novakovic VA, Head JF, Seaton BA, Gilbert GE J Biol Chem. 2008 Mar 14;283(11):7230-41. Epub 2007 Dec 26. PMID:18160406^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Andersen MH, Graversen H, Fedosov SN, Petersen TE, Rasmussen JT. Functional analyses of two cellular binding domains of bovine lactadherin. Biochemistry. 2000 May 23;39(20):6200-6. PMID:10821695
↑ Shao C, Novakovic VA, Head JF, Seaton BA, Gilbert GE. Crystal structure of lactadherin C2 domain at 1.7A resolution with mutational and computational analyses of its membrane-binding motif. J Biol Chem. 2008 Mar 14;283(11):7230-41. Epub 2007 Dec 26. PMID:18160406 doi:10.1074/jbc.M705195200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3bn6"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the C2 Domain of Bovine Lactadherin at 1.67 Angstrom Resolution==
-<StructureSection load='3bn6' size='340' side='right' caption='[[3bn6]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
+<StructureSection load='3bn6' size='340' side='right'caption='[[3bn6]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3bn6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BN6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BN6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3bn6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BN6 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MFGE8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.67&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bn6 OCA], [http://pdbe.org/3bn6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bn6 RCSB], [http://www.ebi.ac.uk/pdbsum/3bn6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bn6 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bn6 OCA], [https://pdbe.org/3bn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bn6 RCSB], [https://www.ebi.ac.uk/pdbsum/3bn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bn6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MFGM_BOVIN MFGM_BOVIN]] Contributes to phagocytic removal of apoptotic cells in many tissues. Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization (By similarity). Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction.<ref>PMID:10821695</ref>
+[https://www.uniprot.org/uniprot/MFGM_BOVIN MFGM_BOVIN] Contributes to phagocytic removal of apoptotic cells in many tissues. Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization (By similarity). Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction.<ref>PMID:10821695</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bn/3bn6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bn/3bn6_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Bovin]]
+[[Category: Bos taurus]]
-[[Category: Gilbert, G E]]
+[[Category: Large Structures]]
-[[Category: Head, J F]]
+[[Category: Gilbert GE]]
-[[Category: Novakovic, V A]]
+[[Category: Head JF]]
-[[Category: Seaton, B A]]
+[[Category: Novakovic VA]]
-[[Category: Shao, C]]
+[[Category: Seaton BA]]
-[[Category: Alternative splicing]]
+[[Category: Shao C]]
-[[Category: Anti-coagulant]]
-[[Category: Anti-coagulation]]
-[[Category: Anticoagulant]]
-[[Category: Anticoagulation]]
-[[Category: Apoptosis]]
-[[Category: Blood clotting]]
-[[Category: Blood coagulation factor v c2 homologue]]
-[[Category: Blood coagulation factor viii c2 homologue]]
-[[Category: Cell adhesion]]
-[[Category: Discoidin domain]]
-[[Category: Egf-like domain]]
-[[Category: F5_f8_type_c]]
-[[Category: Fa58c]]
-[[Category: Fertilization]]
-[[Category: Glycoprotein]]
-[[Category: Membrane binding]]
-[[Category: Milk fat globule]]
-[[Category: Phosphatidyl-serine binding]]
-[[Category: Phosphatidylserine binding]]

3bn6

From Proteopedia

Current revision

Crystal Structure of the C2 Domain of Bovine Lactadherin at 1.67 Angstrom Resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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