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1hxn

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Revision as of 07:30, 7 April 2021

1.8 ANGSTROMS CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF RABBIT SERUM HEMOPEXIN

Structural highlights

1hxn is a 1 chain structure with sequence from Oryctolagus cuniculus. 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

[HEMO_RABIT] Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation.

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

BACKGROUND: Haemopexin is a serum glycoprotein that binds haem reversibly and delivers it to the liver where it is taken up by receptor-mediated endocytosis. Haemopexin has two homologous domains, each having a characteristic fourfold internal sequence repeat. Haemopexin-type domains are also found in other proteins, including the serum adhesion protein vitronectin and various collagenases, in which they mediate protein-protein interactions. RESULTS: We have determined the crystal structure of the C-terminal domain of haemopexin at 1.8 A resolution. The domain is folded into four beta-leaflet modules, arranged in succession around a central pseudo-fourfold axis. A funnel-shaped tunnel through the centre of this disc-shaped domain serves as an ion-binding site. CONCLUSIONS: A model for haem binding by haemopexin is proposed, utilizing an anion-binding site at the wider end of the central tunnel, together with an associated cleft. This parallels the active-site location in other beta-propeller structures. The capacity to bind both cations and anions, together with the disc shape of the domain, suggests that such domains may be used widely for macromolecular recognition.

1.8 A crystal structure of the C-terminal domain of rabbit serum haemopexin.,Faber HR, Groom CR, Baker HM, Morgan WT, Smith A, Baker EN Structure. 1995 Jun 15;3(6):551-9. PMID:8590016^[1]

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

References

↑ Faber HR, Groom CR, Baker HM, Morgan WT, Smith A, Baker EN. 1.8 A crystal structure of the C-terminal domain of rabbit serum haemopexin. Structure. 1995 Jun 15;3(6):551-9. PMID:8590016

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/1hxn"

@@ Line 3: / Line 3: @@
 <StructureSection load='1hxn' size='340' side='right'caption='[[1hxn]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hxn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HXN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HXN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hxn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HXN FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1hxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hxn OCA], [http://pdbe.org/1hxn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hxn RCSB], [http://www.ebi.ac.uk/pdbsum/1hxn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hxn 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=1hxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hxn OCA], [https://pdbe.org/1hxn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hxn RCSB], [https://www.ebi.ac.uk/pdbsum/1hxn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hxn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HEMO_RABIT HEMO_RABIT]] Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation.
+[[https://www.uniprot.org/uniprot/HEMO_RABIT HEMO_RABIT]] Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1hxn

From Proteopedia

Revision as of 07:30, 7 April 2021

1.8 ANGSTROMS CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF RABBIT SERUM HEMOPEXIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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