1ux9: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ux9]] is a 2 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=1UX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UX9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ux9]] is a 2 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=1UX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UX9 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=XE:XENON'>XE</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FC6:HEXACYANOFERRATE(3-)'>FC6</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1umo|1umo]], [[1urv|1urv]], [[1ury|1ury]], [[1ut0|1ut0]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1umo|1umo]], [[1urv|1urv]], [[1ury|1ury]], [[1ut0|1ut0]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ux9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ux9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ux9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ux9 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=1ux9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ux9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ux9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ux9 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/CYGB_HUMAN CYGB_HUMAN]] May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Ascenzi, P | [[Category: Ascenzi, P]] | ||
[[Category: Bolognesi, M | [[Category: Bolognesi, M]] | ||
[[Category: Burmester, T | [[Category: Burmester, T]] | ||
[[Category: Dewilde, S | [[Category: Dewilde, S]] | ||
[[Category: Hankeln, T | [[Category: Hankeln, T]] | ||
[[Category: Moens, L | [[Category: Moens, L]] | ||
[[Category: Pesce, A | [[Category: Pesce, A]] | ||
[[Category: Sanctis, D De | [[Category: Sanctis, D De]] | ||
[[Category: Heme]] | [[Category: Heme]] | ||
[[Category: Oxygen storage/transport]] | [[Category: Oxygen storage/transport]] | ||
[[Category: Oxygen transport]] | [[Category: Oxygen transport]] | ||
[[Category: Transport]] | [[Category: Transport]] | ||
Revision as of 04:10, 25 December 2014
MAPPING PROTEIN MATRIX CAVITIES IN HUMAN CYTOGLOBIN THROUGH XE ATOM BINDING: A CRYSTALLOGRAPHIC INVESTIGATIONMAPPING PROTEIN MATRIX CAVITIES IN HUMAN CYTOGLOBIN THROUGH XE ATOM BINDING: A CRYSTALLOGRAPHIC INVESTIGATION
Structural highlights
Function[CYGB_HUMAN] May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer. 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 PubMedCytoglobin is the fourth recognized globin type, almost ubiquitously distributed in human tissues; its function is still poorly understood. Cytoglobin displays a core region of about 150 residues, structurally related to hemoglobin and myoglobin, and two extra segments, about 20 residues each, at the N- and C-termini. The core region hosts a large apolar cavity, held to provide a ligand diffusion pathway to/from the heme, and/or ligand temporary docking sites. Here we report the crystal structure (2.4A resolution, R-factor 19.1%) of a human cytoglobin mutant bearing the CysB2(38) --> Ser and CysE9(83) --> Ser substitutions (CYGB*), treated under pressurized xenon. Three Xe atoms bind to the heme distal site region of CYGB* mapping the protein matrix apolar cavity. Despite the conserved globin fold, the cavity found in CYGB* is structured differently from those recognized to play a functional role in myoglobin, neuroglobin, truncated hemoglobins, and Cerebratulus lacteus mini-hemoglobin. Mapping protein matrix cavities in human cytoglobin through Xe atom binding.,de Sanctis D, Dewilde S, Pesce A, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M Biochem Biophys Res Commun. 2004 Apr 16;316(4):1217-21. PMID:15044115[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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