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1lfg

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Revision as of 06:44, 29 November 2017

Structure of diferric human lactoferrin

Structural highlights

1lfg is a 1 chain structure with sequence from Human. The January 2016 RCSB PDB Molecule of the Month feature on Siderocalin by David Goodsell is 10.2210/rcsb_pdb/mom_2016_1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TRFL_HUMAN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.^[1] ^[2] Lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration.^[3] ^[4] Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors.^[5] ^[6] The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.^[7] ^[8] Isoform DeltaLf: transcription factor with antiproliferative properties and inducing cell cycle arrest. Binds to DeltaLf response element found in the SKP1, BAX, DCPS, and SELH promoters.^[9] ^[10]

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

The three-dimensional structure of the diferric form of human lactoferrin has been refined at 2.2 A resolution, using synchrotron data combined with a lower resolution (3.2 A) diffractometer data set. Following restrained least-squares refinement and model rebuilding the final model comprises 5330 protein atoms (691 residues), 2Fe(3+) and 2CO(3)(2-) ions, 469 solvent molecules and 98 carbohydrate atoms (eight sugar residues). Root-mean-square deviations from standard geometry are 0.015 A for bond lengths and 0.038 A for angle (1-3) distances, and the final crystallographic R-factor is 0.179 for all 39 113 reflections in the resolution range 8.0-2.2 A. A close structural similarity is seen between the two lobes of the molecule, with differences mainly in loops and turns. The two binding sites are extremely similar, the only apparent differences being a slightly more asymmetric bidentate binding of the carbonate ion to the metal, and a slightly longer Fe-O bond to one of the Tyr ligands, in the N-lobe site relative to the C-lobe site. Distinct differences are seen in the interactions made by two cationic groups, Arg210 and Lys546, behind the iron site, and these may influence the stability of the two metal sites. Analysis of interdomain and interlobe interactions shows that these are few in number which is consistent with the known flexibility of the molecule with respect to domain and lobe movements. Internal water molecules are found in discrete sites and in two large clusters (in the two interdomain clefts) and one tightly bound water molecule is present 3.8 A from the Fe atom in each lobe. The carbohydrate is weakly defined and has been modelled to a limited extent; two sugar residues of the N-lobe glycan and six of the C-lobe glycan. Only one direct protein-carbohydrate contact can be found.

Structure of human diferric lactoferrin refined at 2.2 A resolution.,Haridas M, Anderson BF, Baker EN Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):629-46. PMID:15299793^[11]

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

References

↑ Hendrixson DR, Qiu J, Shewry SC, Fink DL, Petty S, Baker EN, Plaut AG, St Geme JW 3rd. Human milk lactoferrin is a serine protease that cleaves Haemophilus surface proteins at arginine-rich sites. Mol Microbiol. 2003 Feb;47(3):607-17. PMID:12535064
↑ Mariller C, Hardiville S, Hoedt E, Huvent I, Pina-Canseco S, Pierce A. Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor. Biochem Cell Biol. 2012 Jun;90(3):307-19. doi: 10.1139/o11-070. Epub 2012 Feb 9. PMID:22320386 doi:http://dx.doi.org/10.1139/o11-070
↑ Hendrixson DR, Qiu J, Shewry SC, Fink DL, Petty S, Baker EN, Plaut AG, St Geme JW 3rd. Human milk lactoferrin is a serine protease that cleaves Haemophilus surface proteins at arginine-rich sites. Mol Microbiol. 2003 Feb;47(3):607-17. PMID:12535064
↑ Mariller C, Hardiville S, Hoedt E, Huvent I, Pina-Canseco S, Pierce A. Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor. Biochem Cell Biol. 2012 Jun;90(3):307-19. doi: 10.1139/o11-070. Epub 2012 Feb 9. PMID:22320386 doi:http://dx.doi.org/10.1139/o11-070
↑ Hendrixson DR, Qiu J, Shewry SC, Fink DL, Petty S, Baker EN, Plaut AG, St Geme JW 3rd. Human milk lactoferrin is a serine protease that cleaves Haemophilus surface proteins at arginine-rich sites. Mol Microbiol. 2003 Feb;47(3):607-17. PMID:12535064
↑ Mariller C, Hardiville S, Hoedt E, Huvent I, Pina-Canseco S, Pierce A. Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor. Biochem Cell Biol. 2012 Jun;90(3):307-19. doi: 10.1139/o11-070. Epub 2012 Feb 9. PMID:22320386 doi:http://dx.doi.org/10.1139/o11-070
↑ Hendrixson DR, Qiu J, Shewry SC, Fink DL, Petty S, Baker EN, Plaut AG, St Geme JW 3rd. Human milk lactoferrin is a serine protease that cleaves Haemophilus surface proteins at arginine-rich sites. Mol Microbiol. 2003 Feb;47(3):607-17. PMID:12535064
↑ Mariller C, Hardiville S, Hoedt E, Huvent I, Pina-Canseco S, Pierce A. Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor. Biochem Cell Biol. 2012 Jun;90(3):307-19. doi: 10.1139/o11-070. Epub 2012 Feb 9. PMID:22320386 doi:http://dx.doi.org/10.1139/o11-070
↑ Hendrixson DR, Qiu J, Shewry SC, Fink DL, Petty S, Baker EN, Plaut AG, St Geme JW 3rd. Human milk lactoferrin is a serine protease that cleaves Haemophilus surface proteins at arginine-rich sites. Mol Microbiol. 2003 Feb;47(3):607-17. PMID:12535064
↑ Mariller C, Hardiville S, Hoedt E, Huvent I, Pina-Canseco S, Pierce A. Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor. Biochem Cell Biol. 2012 Jun;90(3):307-19. doi: 10.1139/o11-070. Epub 2012 Feb 9. PMID:22320386 doi:http://dx.doi.org/10.1139/o11-070
↑ Haridas M, Anderson BF, Baker EN. Structure of human diferric lactoferrin refined at 2.2 A resolution. Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):629-46. PMID:15299793 doi:10.1107/S0907444994013521

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/1lfg"

@@ Line 1: / Line 1: @@
 ==Structure of diferric human lactoferrin==
 <StructureSection load='1lfg' size='340' side='right' caption='[[1lfg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1lfg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. The January 2016 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Siderocalin''  by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2016_1 10.2210/rcsb_pdb/mom_2016_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LFG FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=1lfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lfg OCA], [http://pdbe.org/1lfg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lfg RCSB], [http://www.ebi.ac.uk/pdbsum/1lfg PDBsum]</span></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=1lfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lfg OCA], [http://pdbe.org/1lfg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lfg RCSB], [http://www.ebi.ac.uk/pdbsum/1lfg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lfg ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 28: @@
 </div>
 <div class="pdbe-citations 1lfg" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Lactoferrin|Lactoferrin]]
 == References ==
 <references/>

1lfg

From Proteopedia

Revision as of 06:44, 29 November 2017

Structure of diferric human lactoferrin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

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