1f4q

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[[Image:1f4q.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF APO GRANCALCIN==
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|PDB= 1f4q |SIZE=350|CAPTION= <scene name='initialview01'>1f4q</scene>, resolution 1.9&Aring;
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<StructureSection load='1f4q' size='340' side='right'caption='[[1f4q]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1f4q]] is a 2 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=1F4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F4Q FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4q OCA], [https://pdbe.org/1f4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f4q RCSB], [https://www.ebi.ac.uk/pdbsum/1f4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f4q ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''CRYSTAL STRUCTURE OF APO GRANCALCIN'''
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[https://www.uniprot.org/uniprot/GRAN_HUMAN GRAN_HUMAN] Calcium-binding protein that may play a role in the adhesion of neutrophils to fibronectin. May play a role in the formation of focal adhesions.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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Grancalcin is a Ca(2+)-binding protein expressed at high level in neutrophils. It belongs to the PEF family, proteins containing five EF-hand motifs and which are known to associate with membranes in Ca(2+)-dependent manner. Prototypic members of this family are Ca(2+)-binding domains of calpain. Our recent finding that grancalcin interacts with L-plastin, a protein known to have actin bundling activity, suggests that grancalcin may play a role in regulation of adherence and migration of neutrophils. The structure of human grancalcin has been determined at 1.9 A resolution in the absence of calcium (R-factor of 0.212 and R-free of 0.249) and at 2. 5 A resolution in the presence of calcium (R-factor of 0.226 and R-free of 0.281). The molecule is predominantly alpha-helical: it contains eight alpha-helices and only two short stretches of two-stranded beta-sheets between the loops of paired EF-hands. Grancalcin forms dimers through the association of the unpaired EF5 hands in a manner similar to that observed in calpain, confirming this mode of association as a paradigm for the PEF family. Only one Ca(2+) was found per dimer under crystallization conditions that included CaCl(2). This cation binds to EF3 in one molecule, while this site in the second molecule of the dimer is unoccupied. This unoccupied site shows higher mobility. The structure determined in the presence of calcium, although does not represent a fully Ca(2+)-loaded form, suggests that calcium induces rather small conformational rearrangements. Comparison with calpain suggests further that the relatively small magnitude of conformational changes invoked by calcium alone may be a characteristic feature of the PEF family. Moreover, the largest differences are localized to the EF1, thus supporting the notion that calcium signaling occurs through this portion of the molecule and that it may involve the N-terminal Gly/Pro rich segment. Electrostatic potential distribution shows significant differences between grancalcin and calpain domain VI demonstrating their distinct character.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f4/1f4q_consurf.spt"</scriptWhenChecked>
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==Disease==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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Known diseases associated with this structure: Cone dystrophy-3 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600364 600364]], Hemolytic anemia due to gamma-glutamylcysteine synthetase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606857 606857]]
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f4q ConSurf].
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1F4Q is a [[Single protein]] structure of 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=1F4Q OCA].
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<div style="clear:both"></div>
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of human grancalcin, a member of the penta-EF-hand protein family., Jia J, Han Q, Borregaard N, Lollike K, Cygler M, J Mol Biol. 2000 Jul 28;300(5):1271-81. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10903868 10903868]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Borregaard, N.]]
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[[Category: Borregaard N]]
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[[Category: Cygler, M.]]
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[[Category: Cygler M]]
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[[Category: Han, Q.]]
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[[Category: Han Q]]
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[[Category: Jia, J.]]
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[[Category: Jia J]]
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[[Category: Lollike, K.]]
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[[Category: Lollike K]]
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[[Category: calcium binding protein]]
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[[Category: penta-ef-hand protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:04:30 2008''
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Current revision

CRYSTAL STRUCTURE OF APO GRANCALCIN

PDB ID 1f4q

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