1ww4: Difference between revisions

Revision as of 16:48, 21 February 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

1WW4 is a Protein complex structure of sequences from Agrocybe cylindracea. 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 Thu Feb 21 15:48:41 2008

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OCA

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-[[Image:1ww4.gif|left|200px]]<br /><applet load="1ww4" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ww4.gif|left|200px]]<br /><applet load="1ww4" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ww4, resolution 2.30&Aring;" />
 '''Agrocybe cylindracea galectin complexed with NeuAca2-3lactose'''<br />
 ==Overview==
-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.
+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 Structure==
-WW4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Agrocybe_cylindracea Agrocybe cylindracea]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WW4 OCA].
+WW4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Agrocybe_cylindracea Agrocybe cylindracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WW4 OCA].
 ==Reference==
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 [[Category: Utsumi, S.]]
 [[Category: Yagi, F.]]
-[[Category: Yoon, H.J.]]
+[[Category: Yoon, H J.]]
 [[Category: agrocybe cylindracea galectin]]
 [[Category: carbohydrate recognition domain]]
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 [[Category: x-ray crystallographic analysis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:42:39 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:48:41 2008''