Lactoferrin: Difference between revisions
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== Function == | == Function == | ||
'''Lactoferrin''' (LTF) is found in secretory fluids. LTF interacts with DNA, RNA, polysaccharides and heparin<ref>PMID:19519436</ref>. For detailed discussion of human lactoferrin see [[Human lactoferrin]]. | '''Lactoferrin''' or '''lactotransferrin''' (LTF) is found in secretory fluids. LTF interacts with DNA, RNA, polysaccharides and heparin<ref>PMID:19519436</ref>. For detailed discussion of human lactoferrin see [[Human lactoferrin]]. | ||
== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
LTF is a bilobal protein with the <scene name='45/455488/Cv/ | LTF is a bilobal protein with the <scene name='45/455488/Cv/7'>N-terminal half and the C-terminal half called N-lobe and C-lobe</scene>. LTF binds with high affinity Fe+3 ion and an anion in both its N-lobe and its C-lobe<ref>PMID:8703903</ref>. The binding site is between the 2 domains of each lobe. | ||
<scene name='45/455488/Cv/ | <scene name='45/455488/Cv/8'>N-lobe binding site</scene>. | ||
The <scene name='45/455488/Cv/ | The <scene name='45/455488/Cv/9'>anion binds the Fe+3 in a 1,2 bidendate fashion</scene>. | ||
<scene name='45/455488/Cv/ | <scene name='45/455488/Cv/10'>C-lobe binding site</scene>. | ||
The <scene name='45/455488/Cv/ | The <scene name='45/455488/Cv/11'>anion binds the Fe+3 in a 1,2 bidendate fashion</scene>. | ||
</StructureSection> | </StructureSection> | ||
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*Apo lactoferrin | *Apo lactoferrin | ||
**[[1cb6]], [[1lfg]], [[1lfh]] – hLTF - human<BR /> | |||
**[[1u62]], [[1xv4]], [[1xv7]], [[1z6v]], [[1z6w]] - hLTF peptide – NMR<BR /> | |||
**[[1i6b]], [[1b7u]] – hoLTF – horse<BR /> | **[[1i6b]], [[1b7u]] – hoLTF – horse<BR /> | ||
**[[1dtz]] – cLTF - camel<BR /> | **[[1dtz]] – cLTF - camel<BR /> | ||
**[[1lfc]] – bLTF residues 17-41 – bovine – NMR<br /> | **[[1lfc]] – bLTF residues 17-41 – bovine – NMR<br /> | ||
**[[4oqo]] – bLTF C lobe<br /> | **[[4oqo]] – bLTF C lobe<br /> | ||
*Lactoferrin | *Lactoferrin | ||
**[[2bjj]], [[1sqy]], [[1n76]]– hLTF + 2Fe<br /> | |||
**[[1b0l]] - hLTF (mutant) + 2Fe<br /> | |||
**[[1fck]] – hLTF + 2Ce<BR /> | |||
**[[1lfi]] - hLTF + 2Cu<BR /> | |||
**[[1lct]] - hLTF N lobe + 2Fe<br /> | |||
**[[1h43]], [[1h44]], [[1h45]], [[1l5t]], [[1eh3]], [[1vfd]], [[1vfe]], [[1hse]], [[1dsn]] - hLTF N lobe (mutant) + 2Fe<br /> | |||
**[[1blf]] – bLTF + 2Fe <BR /> | **[[1blf]] – bLTF + 2Fe <BR /> | ||
**[[1sdx]] - bLTF C lobe + 3Zn<BR /> | **[[1sdx]] - bLTF C lobe + 3Zn<BR /> | ||
**[[5cry]], [[5hbc]], [[7enu]], [[7equ]], [[7ev0]], [[7evq]], [[7fdw]] - bLTF C lobe + Fe+3<br /> | |||
**[[1nkx]], [[3u8q]] - bLTF C lobe + 2Zn + Fe<br /> | **[[1nkx]], [[3u8q]] - bLTF C lobe + 2Zn + Fe<br /> | ||
**[[1b1x]], [[1f9b]] – hoLTF + 2Fe<br /> | **[[1b1x]], [[1f9b]] – hoLTF + 2Fe<br /> | ||
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**[[1ce2]], [[1biy]] – buLTF + 2Fe - buffalo<BR /> | **[[1ce2]], [[1biy]] – buLTF + 2Fe - buffalo<BR /> | ||
**[[1i6q]] – cLTF + 2Fe<br /> | **[[1i6q]] – cLTF + 2Fe<br /> | ||
**[[1jw1]] – LTF + 2Fe – goat | **[[1jw1]] – LTF + 2Fe – goat | ||
*Lactoferrin | *Lactoferrin complex | ||
**[[1bka]] - hLTF + 2Fe + oxalate<BR /> | |||
**[[7jrd]] - hLTF + 2Fe + LTF-binding protein<br /> | |||
**[[7n88]] - hLTF + 2Fe + LTF-binding protein – Cryo EM<br /> | |||
**[[1lcf]] - hLTF + 2Cu + oxalate<BR /> | |||
**[[2pms]] – hLTF N lobe + PSPA transferring-binding domain + 2Zn + 2Fe<br /> | |||
**[[3sdf]] – bLTF C lobe + lipoteichoic acid + 2Zn + Fe<br /> | **[[3sdf]] – bLTF C lobe + lipoteichoic acid + 2Zn + Fe<br /> | ||
**[[4n6p]] - bLTF C lobe + meclofenamic acid + 2Zn + Fe<br /> | **[[4n6p]] - bLTF C lobe + meclofenamic acid + 2Zn + Fe<br /> | ||
| Line 83: | Line 88: | ||
**[[3cr9]] – hoLTF + inhibitor + 2Fe<br /> | **[[3cr9]] – hoLTF + inhibitor + 2Fe<br /> | ||
**[[2j4u]] – cLTF N terminal + OMPC <BR /> | **[[2j4u]] – cLTF N terminal + OMPC <BR /> | ||
}} | }} | ||
Latest revision as of 07:40, 15 June 2023
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3D Structures of lactoferrin
Updated on 15-June-2023
