1a4v: Difference between revisions

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==Overview==

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.

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==

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[[Category: Lactose synthase]]

[[Category: Single protein]]

[[Category: Acharya, K.R.]]

[[Category: Acharya, K R.]]

[[Category: Chandra, N.]]

[[Category: CA]]

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[[Category: lactose synthase]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Lactose synthase]]
 [[Category: Single protein]]
-[[Category: Acharya, K.R.]]
+[[Category: Acharya, K R.]]
 [[Category: Chandra, N.]]
 [[Category: CA]]
@@ Line 21: / Line 21: @@
 [[Category: lactose synthase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:29:03 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:00 2008''