1ttx

From Proteopedia

(Difference between revisions)

Revision as of 06:29, 10 November 2021

Solution Structure of human beta parvalbumin (oncomodulin) refined with a paramagnetism based strategy

Structural highlights

1ttx is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	Homo sapiens (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ONCO_HUMAN] Has some calmodulin-like activity with respect to enzyme activation and growth regulation. Binds two calcium ions.

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

The aim of this research was to determine the structure of human beta-parvalbumin (109 amino acids) and to compare it with its paralog and ortholog proteins. The structure was determined in solution using multinuclear and multidimensional NMR methods and refined using substitution of the EF-hand Ca(2+) ion with a paramagnetic lanthanide. The resulting family of structures had a backbone rmsd of 0.50 A. Comparison with rat oncomodulin (X-ray, 1.3 A resolution) as well as with human (NMR, backbone rmsd of 0.49 A) and rat (X-ray, 2.0 A resolution) parvalbumins reveals small but reliable local differences, often but not always related to amino acid variability. The analysis of these structures has led us to propose an explanation for the different affinity for Ca(2+) between alpha- and beta-parvalbumins and between parvalbumins and calmodulins.

Solution structure of human beta-parvalbumin and structural comparison with its paralog alpha-parvalbumin and with their rat orthologs.,Babini E, Bertini I, Capozzi F, Del Bianco C, Hollender D, Kiss T, Luchinat C, Quattrone A Biochemistry. 2004 Dec 28;43(51):16076-85. PMID:15610002^[1]

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

References

↑ Babini E, Bertini I, Capozzi F, Del Bianco C, Hollender D, Kiss T, Luchinat C, Quattrone A. Solution structure of human beta-parvalbumin and structural comparison with its paralog alpha-parvalbumin and with their rat orthologs. Biochemistry. 2004 Dec 28;43(51):16076-85. PMID:15610002 doi:10.1021/bi048388o

1 Structural highlights
2 Function
3 Evolutionary Conservation
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/1ttx"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ttx' size='340' side='right'caption='[[1ttx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ttx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TTX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TTX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ttx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TTX FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Homo sapiens ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Homo sapiens ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ttx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ttx OCA], [http://pdbe.org/1ttx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ttx RCSB], [http://www.ebi.ac.uk/pdbsum/1ttx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ttx 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=1ttx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ttx OCA], [https://pdbe.org/1ttx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ttx RCSB], [https://www.ebi.ac.uk/pdbsum/1ttx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ttx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ONCO_HUMAN ONCO_HUMAN]] Has some calmodulin-like activity with respect to enzyme activation and growth regulation. Binds two calcium ions.
+[[https://www.uniprot.org/uniprot/ONCO_HUMAN ONCO_HUMAN]] Has some calmodulin-like activity with respect to enzyme activation and growth regulation. Binds two calcium ions.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1ttx

From Proteopedia

Revision as of 06:29, 10 November 2021

Solution Structure of human beta parvalbumin (oncomodulin) refined with a paramagnetism based strategy

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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