1nub

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[[Image:1nub.gif|left|200px]]
 
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{{Structure
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==HELIX C DELETION MUTANT OF BM-40 FS-EC DOMAIN PAIR==
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|PDB= 1nub |SIZE=350|CAPTION= <scene name='initialview01'>1nub</scene>, resolution 2.80&Aring;
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<StructureSection load='1nub' size='340' side='right'caption='[[1nub]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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<table><tr><td colspan='2'>[[1nub]] 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=1NUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NUB 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]] 2.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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}}
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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=1nub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nub OCA], [https://pdbe.org/1nub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nub RCSB], [https://www.ebi.ac.uk/pdbsum/1nub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nub ProSAT]</span></td></tr>
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</table>
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'''HELIX C DELETION MUTANT OF BM-40 FS-EC DOMAIN PAIR'''
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== Function ==
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[https://www.uniprot.org/uniprot/SPRC_HUMAN SPRC_HUMAN] Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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The extracellular calcium-binding domain (positions 138-286) of the matrix protein BM-40 possesses a binding epitope of moderate affinity for several collagen types. This epitope was predicted to reside in helix alphaA and to be partially masked by helix alphaC. Here we show that deletion of helix alphaC produces a 10-fold increase in collagen affinity similar to that seen after proteolytic cleavage of this helix. The predicted removal of the steric constraint was clearly demonstrated by the crystal structure of the mutant at 2.8 A resolution. This constitutively activated mutant was used to map the collagen-binding site following alanine mutagenesis at 13 positions. Five residues were crucial for binding, R149 and N156 in helix alphaA, and L242, M245 and E246 in a loop region connecting the two EF hands of BM-40. These residues are spatially close and form a flat ring of 15 A diameter which matches the diameter of a triple-helical collagen domain. The mutations showed similar effects on binding to collagens I and IV, indicating nearly identical binding sites on both collagens. Selected mutations in the non-activated mutant DeltaI also reduced collagen binding, consistent with the same location of the epitope but in a more cryptic form in intact BM-40.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nu/1nub_consurf.spt"</scriptWhenChecked>
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1NUB 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=1NUB OCA].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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Crystal structure and mapping by site-directed mutagenesis of the collagen-binding epitope of an activated form of BM-40/SPARC/osteonectin., Sasaki T, Hohenester E, Gohring W, Timpl R, EMBO J. 1998 Mar 16;17(6):1625-34. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9501084 9501084]
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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=1nub ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[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: Hohenester, E.]]
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[[Category: Hohenester E]]
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[[Category: Sasaki, T.]]
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[[Category: Sasaki T]]
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[[Category: Timpl, R.]]
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[[Category: Timpl R]]
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[[Category: CA]]
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[[Category: anti-adhesive protein]]
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[[Category: collagen binding]]
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[[Category: extracellular module]]
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[[Category: glycoprotein]]
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[[Category: glycosylated protein]]
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[[Category: site-directed mutagenesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:01:46 2008''
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Current revision

HELIX C DELETION MUTANT OF BM-40 FS-EC DOMAIN PAIR

PDB ID 1nub

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