1A4V

ALPHA-LACTALBUMIN

Summary for 1A4V

• Entry DOI: 10.2210/pdb1a4v/pdb
• Descriptor: ALPHA-LACTALBUMIN, CALCIUM ION (3 entities in total)
• Functional Keywords: lactose synthase, calcium binding, alpha-lactalbumin
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 14173.28

Authors

Chandra, N.,Acharya, K.R. (deposition date: 1998-02-05, release date: 1999-04-27, Last modification date: 2024-10-23)

Primary citation

Chandra, N.,Brew, K.,Acharya, K.R.
Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin.
Biochemistry, 37:4767-4772, 1998

PubMed Abstract: 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.

PubMed: 9537992
DOI: 10.1021/bi973000t

Experimental method

X-RAY DIFFRACTION (1.8 Å)