3ve1
From Proteopedia
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{{STRUCTURE_3ve1| PDB=3ve1 | SCENE= }} | {{STRUCTURE_3ve1| PDB=3ve1 | SCENE= }} | ||
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===The 2.9 angstrom crystal structure of Transferrin binding protein B (TbpB) from serogroup B M982 Neisseria meningitidis in complex with human transferrin=== | ===The 2.9 angstrom crystal structure of Transferrin binding protein B (TbpB) from serogroup B M982 Neisseria meningitidis in complex with human transferrin=== | ||
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{{ABSTRACT_PUBMED_22343719}} | {{ABSTRACT_PUBMED_22343719}} | ||
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| + | ==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> | ||
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| + | ==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. | ||
==About this Structure== | ==About this Structure== | ||
[[3ve1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_b Neisseria meningitidis serogroup b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VE1 OCA]. | [[3ve1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_b Neisseria meningitidis serogroup b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VE1 OCA]. | ||
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| + | ==Reference== | ||
| + | <references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Neisseria meningitidis serogroup b]] | [[Category: Neisseria meningitidis serogroup b]] | ||
Revision as of 08:54, 24 March 2013
Contents |
The 2.9 angstrom crystal structure of Transferrin binding protein B (TbpB) from serogroup B M982 Neisseria meningitidis in complex with human transferrin
Template:ABSTRACT PUBMED 22343719
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.
About this Structure
3ve1 is a 4 chain structure with sequence from Homo sapiens and Neisseria meningitidis serogroup b. Full crystallographic information is available from OCA.
Reference
- ↑ 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
