1CVN

CONCANAVALIN A COMPLEXED TO TRIMANNOSIDE

1CVN の概要

• エントリーDOI: 10.2210/pdb1cvn/pdb
• 分子名称: CONCANAVALIN A, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: concanavalin a, saccharide binding, lectin (agglutinin)
• 由来する生物種: Canavalia ensiformis (jack bean)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 104887.36

構造登録者

Naismith, J.H. (登録日: 1995-08-09, 公開日: 1996-10-14, 最終更新日: 2024-05-22)

主引用文献

Naismith, J.H.,Field, R.A.
Structural basis of trimannoside recognition by concanavalin A.
J.Biol.Chem., 271:972-976, 1996

PubMed Abstract: Despite the fact that complex saccharides play an important role in many biological recognition processes, molecular level descriptions of protein-carbohydrate interactions are sparse. The legume lectin concanavalin A (con A), from Canavalia ensiformis, specifically recognizes the trimannoside core of many complex glycans. We have determined the crystal structure of a con A-trimannoside complex at 2.3-A resolution now describe the trimannoside interaction with conA. All three sugar residues are in well defined difference electron density. The 1,6-linked mannose residue is bound at the previously reported monosaccharide binding site; the other two sugars bind in an extended cleft formed by residues Tyr-12, Pro-13, Asn-14, Thr-15, and Asp-16. Hydrogen bonds are formed between the protein and all three sugar residues. In particular, the 1,3-linked mannose residue makes a strong hydrogen bond with the main chain of the protein. In addition, a water molecule, which is conserved in other con A structures, plays an important role in anchoring the reducing sugar unit to the protein. The complex is further stabilized by van der Waals interactions. The structure provides a rationale for the high affinity of con A for N-linked glycans.

PubMed: 8557713
DOI: 10.1074/jbc.271.2.972

実験手法

X-RAY DIFFRACTION (2.3 Å)