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[[Image:1a4v.gif|left|200px]]
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{{STRUCTURE_1a4v|  PDB=1a4v  |  SCENE=  }}
'''ALPHA-LACTALBUMIN'''


==ALPHA-LACTALBUMIN==
<StructureSection load='1a4v' size='340' side='right'caption='[[1a4v]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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='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>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a4/1a4v_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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:9537992<ref>PMID:9537992</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1a4v" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Lactose synthase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Acharya KR]]
[[Category: Acharya, K R.]]
[[Category: Chandra N]]
[[Category: Chandra, N.]]
[[Category: Alpha-lactalbumin]]
[[Category: Calcium binding]]
[[Category: Lactose synthase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:48:53 2008''

Latest revision as of 07:14, 23 October 2024

ALPHA-LACTALBUMIN

1a4v, resolution 1.80Å

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