Crystal structure of a conger eel galectin (congerin II) at 1.45A resolution: implication for the accelerated evolution of a new ligand-binding site following gene duplication (Q27639567)

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English	Crystal structure of a conger eel galectin (congerin II) at 1.45A resolution: implication for the accelerated evolution of a new ligand-binding site following gene duplication	scientific article

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scholarly article

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Crystal structure of a conger eel galectin (congerin II) at 1.45A resolution: implication for the accelerated evolution of a new ligand-binding site following gene duplication (English)

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crystal structure

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based on heuristic

inferred from title

gene duplication

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based on heuristic

inferred from title

author name string

Tsuyoshi Shirai

1

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Yuuka Matsui

2

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Clara Shionyu-Mitsuyama

3

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Takashi Yamane

4

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Hisao Kamiya

5

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Chihiro Ishii

6

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Tomohisa Ogawa

7

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Koji Muramoto

8

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language of work or name

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publication date

30 August 2002

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Journal of Molecular Biology

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321

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5

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879-89

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Purification and properties of agglutinins from conger eel, Conger Myriaster (Brevoort), skin mucus

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The amino-acid sequence of a lectin from conger eel, Conger myriaster, skin mucus

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Functional and structural characterization of multiple galectins from the skin mucus of conger eel, Conger myriaster

1 reference

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Accelerated evolution in the protein-coding region of galectin cDNAs, congerin I and congerin II, from skin mucus of conger eel (Conger myriaster)

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1 reference

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Large-scale search for genes on which positive selection may operate

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Statistical methods for detecting molecular adaptation

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Accelerated evolution in the reactive centre regions of serine protease inhibitors

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Pattern of nucleotide substitution at major histocompatibility complex class I loci reveals overdominant selection

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High-level expression and characterization of fully active recombinant conger eel galectins in Eschericia coli.

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AMoRe: an automated package for molecular replacement

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PROCHECK: a program to check the stereochemical quality of protein structures

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DNA data bank of Japan (DDBJ) in collaboration with mass sequencing teams

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The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000.

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A simple method for estimating evolutionary rates of base substitutions through comparative studies of nucleotide sequences

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10.1016/S0022-2836(02)00700-3

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