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Legume lectin

Legume lectin domain (or L-type lectin domain)
Structure of the monosaccharide binding site of lentil lectin.[1]
Identifiers
SymbolLectin_legB
PfamPF00139
Pfam clanCL0004
InterProIPR001220
PROSITEPDOC00278
SCOP21lem / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1apn​, 1avb​, 1ax0​, 1ax1​, 1ax2​, 1axy​, 1axz​, 1azd​, 1bjq​, 1bqp​, 1bxh​, 1bzw​, 1ces​, 1ciw​, 1cjp​, 1cn1​, 1con​, 1cq9​, 1cr7​, 1cvn​, 1dbn​, 1dgl​, 1dhk​, 1dq0​, 1dq1​, 1dq2​, 1dq4​, 1dq5​, 1dq6​, 1dzq​, 1enq​, 1enr​, 1ens​, 1f9k​, 1fat​, 1fay​, 1fny​, 1fnz​, 1fx5​, 1fyu​, 1g7y​, 1g8w​, 1g9f​, 1gic​, 1gkb​, 1gnz​, 1gsl​, 1gz9​, 1gzc​, 1h9p​, 1h9w​, 1hkd​, 1hql​, 1hqw​, 1i3h​, 1ioa​, 1jbc​, 1jn2​, 1joj​, 1jui​, 1jw6​, 1jxn​, 1jyc​, 1jyi​, 1lec​, 1led​, 1lem​, 1len​, 1les​, 1lgb​, 1lgc​, 1loa​, 1lob​, 1loc​, 1lod​, 1loe​, 1lof​, 1log​, 1lte​, 1lu1​, 1lu2​, 1lul​, 1mvq​, 1n3o​, 1n3p​, 1n3q​, 1n47​, 1nls​, 1nxd​, 1ofs​, 1ona​, 1q8o​, 1q8p​, 1q8q​, 1q8s​, 1q8v​, 1qdc​, 1qdo​, 1qf3​, 1qgl​, 1qmo​, 1qnw​, 1qny​, 1qoo​, 1qos​, 1qot​, 1rin​, 1rir​, 1rit​, 1s1a​, 1sbd​, 1sbe​, 1sbf​, 1scr​, 1scs​, 1sfy​, 1tei​, 1ukg​, 1uzy​, 1uzz​, 1v00​, 1v6i​, 1v6j​, 1v6k​, 1v6l​, 1v6m​, 1v6n​, 1v6o​, 1val​, 1vam​, 1viw​, 1vln​, 1wbf​, 1wbl​, 1wuv​, 2a7a​, 2ar6​, 2arb​, 2are​, 2arx​, 2auy​, 2b7y​, 2bqp​, 2cna​, 2ctv​, 2cwm​, 2cy6​, 2cyf​, 2d3p​, 2d3r​, 2d3s​, 2d7f​, 2dh1​, 2dtw​, 2dty​, 2du0​, 2du1​, 2dv9​, 2dva​, 2dvb​, 2dvd​, 2dvf​, 2dvg​, 2e51​, 2e53​, 2e7q​, 2e7t​, 2ef6​, 2eig​, 2enr​, 2fmd​, 2g4i​, 2gdf​, 2gme​, 2gmm​, 2gmp​, 2gn3​, 2gn7​, 2gnb​, 2gnd​, 2gnm​, 2gnt​, 2jdz​, 2je7​, 2je9​, 2jec​, 2lal​, 2ltn​, 2ovu​, 2ow4​, 2p2k​, 2p34​, 2p37​, 2pel​, 2phf​, 2phr​, 2pht​, 2phu​, 2phw​, 2phx​, 2sba​, 2tep​, 2uu8​, 2zbj​, 2zmk​, 2zml​, 2zmn​, 3cna​, 3d4k​, 3enr​, 5cna

The legume lectins (or L-type lectins) are a family of sugar-binding proteins or lectins found in the seeds and, in smaller amounts, in the roots, stems, leaves and bark of plants of the family Fabaceae.[2][3] The exact function of the legume lectins in vivo is unknown but they are probably involved in the defense of plants against predators. Related proteins in other plant families and in animals have also been found. They have been used for decades as a model system for the study of protein-carbohydrate interactions, because they show a wide variety of binding specificities and are easy to obtain, purify, and characterize the structure of.[3] Well-studied members of this protein family include phytohemagglutinin, soybean agglutinins, and concanavalin A.

  1. ^ Loris R, Casset F, Bouckaert J, et al. (December 1994). "The monosaccharide binding site of lentil lectin: an X-ray and molecular modelling study". Glycoconj. J. 11 (6): 507–17. doi:10.1007/bf00731301. PMID 7696853. S2CID 20037257.
  2. ^ Sharon N, Lis H (November 1990). "Legume lectins--a large family of homologous proteins". FASEB J. 4 (14): 3198–208. doi:10.1096/fasebj.4.14.2227211. PMID 2227211. S2CID 23310019.
  3. ^ a b Loris R, Hamelryck T, Bouckaert J, Wyns L (March 1998). "Legume lectin structure". Biochim. Biophys. Acta. 1383 (1): 9–36. doi:10.1016/S0167-4838(97)00182-9. PMID 9546043.

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Lectine de légumineuses French Легумин Russian

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