1ww4: Difference between revisions
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'''Agrocybe cylindracea galectin complexed with NeuAca2-3lactose''' | '''Agrocybe cylindracea galectin complexed with NeuAca2-3lactose''' | ||
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==About this Structure== | ==About this Structure== | ||
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WW4 OCA]. | |||
==Reference== | ==Reference== | ||
Structural basis of a fungal galectin from Agrocybe cylindracea for recognizing sialoconjugate., Ban M, Yoon HJ, Demirkan E, Utsumi S, Mikami B, Yagi F, J Mol Biol. 2005 Aug 26;351(4):695-706. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16051274 16051274] | Structural basis of a fungal galectin from Agrocybe cylindracea for recognizing sialoconjugate., Ban M, Yoon HJ, Demirkan E, Utsumi S, Mikami B, Yagi F, J Mol Biol. 2005 Aug 26;351(4):695-706. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16051274 16051274] | ||
[[Category: Ban, M.]] | [[Category: Ban, M.]] | ||
[[Category: Demirkan, E.]] | [[Category: Demirkan, E.]] | ||
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[[Category: Yagi, F.]] | [[Category: Yagi, F.]] | ||
[[Category: Yoon, H J.]] | [[Category: Yoon, H J.]] | ||
[[Category: | [[Category: Agrocybe cylindracea galectin]] | ||
[[Category: | [[Category: Carbohydrate recognition domain]] | ||
[[Category: | [[Category: Fungal galectin]] | ||
[[Category: | [[Category: N-acetylneuraminyl lactose]] | ||
[[Category: | [[Category: X-ray crystallographic analysis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:12:51 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 14:12, 3 May 2008
Agrocybe cylindracea galectin complexed with NeuAca2-3lactose
OverviewOverview
Galectin from an edible fungus Agrocybe cylindracea (ACG) has a strong preference for N-acetylneuraminyl lactose (NeuAcalpha2-3lactose). The sugar recognition mechanism of ACG was explored by the X-ray crystallographic analyses of ligand-free ACG, and its complex with lactose, 3'-sulfonyl lactose and NeuAcalpha2-3lactose. The refined structure shows that ACG is a "proto"-type galectin composed of a beta-sandwich of two antiparallel sheets, each with six strands, in contrast to the five and six strands in animal galectins. ACG dimer in solution was classified as being among the "layer"-type. The carbohydrate recognition domain (CRD) of this galectin is common to those of animal galectins, except for substitution of one residue, Ala64, which corresponds to Asn46 in human galectin 1. A five-residue insertion in ACG at positions 42-46 involving Ser44 and Asn46 modified the architecture of the sugar binding site that contributes sialic acid specificity. Furthermore, it was found that the binding of a sulfate ion near the CRD in the ligand-free form led to a change in the conformation of the loop region caused by main-chain cis/trans transition between Ser44 and Pro45.
About this StructureAbout this Structure
Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of a fungal galectin from Agrocybe cylindracea for recognizing sialoconjugate., Ban M, Yoon HJ, Demirkan E, Utsumi S, Mikami B, Yagi F, J Mol Biol. 2005 Aug 26;351(4):695-706. PMID:16051274 Page seeded by OCA on Sat May 3 14:12:51 2008