1a3k: Difference between revisions

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[[Image:1a3k.gif|left|200px]]<br />

[[Image:1a3k.gif|left|200px]]<br /><applet load="1a3k" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1a3k" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1a3k, resolution 2.1Å" />

'''X-RAY CRYSTAL STRUCTURE OF THE HUMAN GALECTIN-3 CARBOHYDRATE RECOGNITION DOMAIN (CRD) AT 2.1 ANGSTROM RESOLUTION'''<br />

==Overview==

Galectins are a family of lectins which share similar carbohydrate, recognition domains (CRDs) and affinity for small beta-galactosides, but, which show significant differences in binding specificity for more complex, glycoconjugates. We report here the x-ray crystal structure of the human, galectin-3 CRD, in complex with lactose and N-acetyllactosamine, at 2.1-A, resolution. This structure represents the first example of a CRD, determined from a galectin which does not show the canonical 2-fold, symmetric dimer organization. Comparison with the published structures of, galectins-1 and -2 provides an explanation for the differences in, carbohydrate-binding specificity shown by galectin-3, and for the fact, that it fails to form dimers by analogous CRD-CRD interactions.

Galectins are a family of lectins which share similar carbohydrate recognition domains (CRDs) and affinity for small beta-galactosides, but which show significant differences in binding specificity for more complex glycoconjugates. We report here the x-ray crystal structure of the human galectin-3 CRD, in complex with lactose and N-acetyllactosamine, at 2.1-A resolution. This structure represents the first example of a CRD determined from a galectin which does not show the canonical 2-fold symmetric dimer organization. Comparison with the published structures of galectins-1 and -2 provides an explanation for the differences in carbohydrate-binding specificity shown by galectin-3, and for the fact that it fails to form dimers by analogous CRD-CRD interactions.

==About this Structure==

1A3K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1A3K OCA].

1A3K is a [http://en.wikipedia.org/wiki/Single_protein 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=1A3K OCA].

==Reference==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Barondes, S.H.]]

[[Category: Barondes, S H.]]

[[Category: Kanigsberg, A.]]

[[Category: Leffler, H.]]

[[Category: Rini, J.M.]]

[[Category: Rini, J M.]]

[[Category: Seetharaman, J.]]

[[Category: Slaaby, R.]]

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[[Category: lectin]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 15~~:55:~~06 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:27 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1a3k.gif|left|200px]]<br />
+[[Image:1a3k.gif|left|200px]]<br /><applet load="1a3k" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1a3k" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1a3k, resolution 2.1&Aring;" />
 '''X-RAY CRYSTAL STRUCTURE OF THE HUMAN GALECTIN-3 CARBOHYDRATE RECOGNITION DOMAIN (CRD) AT 2.1 ANGSTROM RESOLUTION'''<br />
 ==Overview==
-Galectins are a family of lectins which share similar carbohydrate, recognition domains (CRDs) and affinity for small beta-galactosides, but, which show significant differences in binding specificity for more complex, glycoconjugates. We report here the x-ray crystal structure of the human, galectin-3 CRD, in complex with lactose and N-acetyllactosamine, at 2.1-A, resolution. This structure represents the first example of a CRD, determined from a galectin which does not show the canonical 2-fold, symmetric dimer organization. Comparison with the published structures of, galectins-1 and -2 provides an explanation for the differences in, carbohydrate-binding specificity shown by galectin-3, and for the fact, that it fails to form dimers by analogous CRD-CRD interactions.
+Galectins are a family of lectins which share similar carbohydrate recognition domains (CRDs) and affinity for small beta-galactosides, but which show significant differences in binding specificity for more complex glycoconjugates. We report here the x-ray crystal structure of the human galectin-3 CRD, in complex with lactose and N-acetyllactosamine, at 2.1-A resolution. This structure represents the first example of a CRD determined from a galectin which does not show the canonical 2-fold symmetric dimer organization. Comparison with the published structures of galectins-1 and -2 provides an explanation for the differences in carbohydrate-binding specificity shown by galectin-3, and for the fact that it fails to form dimers by analogous CRD-CRD interactions.
 ==About this Structure==
-A3K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A3K OCA].
+A3K is a [http://en.wikipedia.org/wiki/Single_protein 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=1A3K OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Barondes, S.H.]]
+[[Category: Barondes, S H.]]
 [[Category: Kanigsberg, A.]]
 [[Category: Leffler, H.]]
-[[Category: Rini, J.M.]]
+[[Category: Rini, J M.]]
 [[Category: Seetharaman, J.]]
 [[Category: Slaaby, R.]]
@@ Line 25: / Line 24: @@
 [[Category: lectin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 15:55:06 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:27 2008''