1hml

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{{Seed}}
 
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[[Image:1hml.png|left|200px]]
 
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==ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE==
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The line below this paragraph, containing "STRUCTURE_1hml", creates the "Structure Box" on the page.
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<StructureSection load='1hml' size='340' side='right'caption='[[1hml]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1hml]] 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=1HML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HML FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.7&#8491;</td></tr>
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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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1hml| PDB=1hml | SCENE= }}
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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=1hml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hml OCA], [https://pdbe.org/1hml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hml RCSB], [https://www.ebi.ac.uk/pdbsum/1hml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hml 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/hm/1hml_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1hml ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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It has been proposed that the binding of Zn2+ to alpha-lactalbumin switches the conformation to one akin to a state intermediate in the folding of the protein. However, the high resolution x-ray crystal structure of human alpha-lactalbumin-Zn2+ complex at 1.7-A resolution (pH 7.6) does not reveal any significant change in conformation from the native state. The Zn2+ ion binds specifically in the "cleft" of alpha-lactalbumin (the region which forms the active site of the homologous protein lysozyme). This may suggest a possible role for Zn2+ binding in lactose synthase complex. The coordination of the Zn2+ ion involves a symmetry-related molecule in the crystal, the crystal contacts being stabilized by a SO4(2-) ion bound at the interface between three molecules.
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===ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE===
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Alpha-lactalbumin possesses a distinct zinc binding site.,Ren J, Stuart DI, Acharya KR J Biol Chem. 1993 Sep 15;268(26):19292-8. PMID:8366079<ref>PMID:8366079</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1hml" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_8366079}}, adds the Publication Abstract to the page
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*[[Alpha-lactalbumin|Alpha-lactalbumin]]
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(as it appears on PubMed at http://www.pubmed.gov), where 8366079 is the PubMed ID number.
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*[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_8366079}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1HML 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=1HML OCA].
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==Reference==
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Alpha-lactalbumin possesses a distinct zinc binding site., Ren J, Stuart DI, Acharya KR, J Biol Chem. 1993 Sep 15;268(26):19292-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8366079 8366079]
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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: Ren J]]
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[[Category: Ren, J.]]
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[[Category: Stuart DI]]
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[[Category: Stuart, D I.]]
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[[Category: Calcium-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:24:19 2008''
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Current revision

ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE

PDB ID 1hml

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