1a4v

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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].
</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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== Publication Abstract from PubMed ==
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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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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>
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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 class="pdbe-citations 1a4v" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
*[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]]
*[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]]
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 05:23, 5 June 2024

ALPHA-LACTALBUMIN

PDB ID 1a4v

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