4x1b

From Proteopedia

(Difference between revisions)

Revision as of 21:06, 12 April 2023

Human serum transferrin with ferric ion bound at the C-lobe only

Structural highlights

4x1b is a 1 chain structure with sequence from Homo sapiens. 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

Disease

TRFE_HUMAN Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:209300. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.^[1] ^[2]

Function

TRFE_HUMAN Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.

Publication Abstract from PubMed

X-ray crystal structures of human serum transferrin (77 kDa) with YbIII or FeIII bound to the C-lobe and malonate as the synergistic anion show that the large YbIII ion causes the expansion of the metal binding pocket while octahedral metal coordination geometry is preserved, an unusual geometry for a lanthanide ion.

"Anion clamp" allows flexible protein to impose coordination geometry on metal ions.,Wang M, Lai TP, Wang L, Zhang H, Yang N, Sadler PJ, Sun H Chem Commun (Camb). 2015 Apr 9. PMID:25854324^[3]

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

References

↑ Beutler E, Gelbart T, Lee P, Trevino R, Fernandez MA, Fairbanks VF. Molecular characterization of a case of atransferrinemia. Blood. 2000 Dec 15;96(13):4071-4. PMID:11110675
↑ Knisely AS, Gelbart T, Beutler E. Molecular characterization of a third case of human atransferrinemia. Blood. 2004 Oct 15;104(8):2607. PMID:15466165 doi:10.1182/blood-2004-05-1751
↑ Wang M, Lai TP, Wang L, Zhang H, Yang N, Sadler PJ, Sun H. "Anion clamp" allows flexible protein to impose coordination geometry on metal ions. Chem Commun (Camb). 2015 Apr 9. PMID:25854324 doi:http://dx.doi.org/10.1039/c4cc09642h

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4x1b"

Categories: Homo sapiens | Large Structures | Sun H | Wang M | Zhang H

@@ Line 3: / Line 3: @@
 <StructureSection load='4x1b' size='340' side='right'caption='[[4x1b]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4x1b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X1B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X1B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4x1b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X1B FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4x1d|4x1d]]</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=4x1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x1b OCA], [https://pdbe.org/4x1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x1b RCSB], [https://www.ebi.ac.uk/pdbsum/4x1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x1b ProSAT]</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=4x1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x1b OCA], [http://pdbe.org/4x1b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x1b RCSB], [http://www.ebi.ac.uk/pdbsum/4x1b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x1b ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[http://omim.org/entry/209300 209300]]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>PMID:11110675</ref> <ref>PMID:15466165</ref>
+[https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[https://omim.org/entry/209300 209300]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>PMID:11110675</ref> <ref>PMID:15466165</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
+[https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 ==See Also==
-*[[Transferrin|Transferrin]]
+*[[Transferrin 3D structures|Transferrin 3D structures]]
 == References ==
 <references/>
@@ Line 30: / Line 29: @@
 [[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Sun, H]]
+[[Category: Sun H]]
-[[Category: Wang, M]]
+[[Category: Wang M]]
-[[Category: Zhang, H]]
+[[Category: Zhang H]]
-[[Category: Ferric]]
-[[Category: Malonate]]
-[[Category: Metal transport]]
-[[Category: Transferrin]]
-[[Category: Ytterbium]]

4x1b

From Proteopedia

Revision as of 21:06, 12 April 2023

Human serum transferrin with ferric ion bound at the C-lobe only

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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