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1a4v

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[[Image:1a4v.gif|left|200px]]
 
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{{Structure
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==ALPHA-LACTALBUMIN==
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|PDB= 1a4v |SIZE=350|CAPTION= <scene name='initialview01'>1a4v</scene>, resolution 1.8&Aring;
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<StructureSection load='1a4v' size='340' side='right'caption='[[1a4v]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE= <scene name='pdbsite=CB1:Ca+Binding+Site+In+The+Ca-Binding-Elbow+Region+Is+Referr+...'>CB1</scene> and <scene name='pdbsite=CB2:This+Is+The+Secondary+Ca+Binding+Site.+At+This+Site+The+...'>CB2</scene>
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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'>[[1a4v]] is a 1 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=1A4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A4V FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Lactose_synthase Lactose synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.22 2.4.1.22]
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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]] 1.8&#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></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=1a4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4v OCA], [https://pdbe.org/1a4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a4v RCSB], [https://www.ebi.ac.uk/pdbsum/1a4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a4v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LALBA_HUMAN LALBA_HUMAN] Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a4/1a4v_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=1a4v ConSurf].
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<div style="clear:both"></div>
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'''ALPHA-LACTALBUMIN'''
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==See Also==
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*[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8 A) in the presence of an elevated level of calcium reveals a new secondary calcium binding site, 7.9 A away from the primary calcium binding site known in all alpha-lactalbumin structures so far. The new calcium binding site is different from the zinc and sulfate binding sites [Ren, J., et al. (1993) J. Biol. Chem. 268, 19292-19298] but shares common features with the manganese binding site as described by Gerkin [Gerkin, T. A. (1984) Biochemistry 23, 4688-4697]. The proximity of the manganese and calcium binding region and the location of the functional site on one side of the charged surface of the alpha-lactalbumin molecule suggest that these binding sites might play a role in the formation of the lactose synthase complex.
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==About this Structure==
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1A4V 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=1A4V OCA].
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==Reference==
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Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin., Chandra N, Brew K, Acharya KR, Biochemistry. 1998 Apr 7;37(14):4767-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9537992 9537992]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Lactose synthase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Acharya KR]]
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[[Category: Acharya, K R.]]
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[[Category: Chandra N]]
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[[Category: Chandra, N.]]
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[[Category: CA]]
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[[Category: alpha-lactalbumin]]
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[[Category: calcium binding]]
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[[Category: lactose synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:52:57 2008''
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Current revision

ALPHA-LACTALBUMIN

PDB ID 1a4v

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