1a3k
From Proteopedia
(New page: 200px<br /> <applet load="1a3k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a3k, resolution 2.1Å" /> '''X-RAY CRYSTAL STRUCT...) |
|||
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=" | + | |
caption="1a3k, resolution 2.1Å" /> | caption="1a3k, resolution 2.1Å" /> | ||
'''X-RAY CRYSTAL STRUCTURE OF THE HUMAN GALECTIN-3 CARBOHYDRATE RECOGNITION DOMAIN (CRD) AT 2.1 ANGSTROM RESOLUTION'''<br /> | '''X-RAY CRYSTAL STRUCTURE OF THE HUMAN GALECTIN-3 CARBOHYDRATE RECOGNITION DOMAIN (CRD) AT 2.1 ANGSTROM RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
- | Galectins are a family of lectins which share similar carbohydrate | + | 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== | ==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:// | + | 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== | ==Reference== | ||
Line 14: | Line 13: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Barondes, S | + | [[Category: Barondes, S H.]] |
[[Category: Kanigsberg, A.]] | [[Category: Kanigsberg, A.]] | ||
[[Category: Leffler, H.]] | [[Category: Leffler, H.]] | ||
- | [[Category: Rini, J | + | [[Category: Rini, J M.]] |
[[Category: Seetharaman, J.]] | [[Category: Seetharaman, J.]] | ||
[[Category: Slaaby, R.]] | [[Category: Slaaby, R.]] | ||
Line 25: | Line 24: | ||
[[Category: lectin]] | [[Category: lectin]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:27 2008'' |
Revision as of 09:40, 21 February 2008
|
X-RAY CRYSTAL STRUCTURE OF THE HUMAN GALECTIN-3 CARBOHYDRATE RECOGNITION DOMAIN (CRD) AT 2.1 ANGSTROM RESOLUTION
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.
About this Structure
1A3K is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution., Seetharaman J, Kanigsberg A, Slaaby R, Leffler H, Barondes SH, Rini JM, J Biol Chem. 1998 May 22;273(21):13047-52. PMID:9582341
Page seeded by OCA on Thu Feb 21 11:40:27 2008