1S1N

SH3 domain of human nephrocystin

1S1N の概要

• エントリーDOI: 10.2210/pdb1s1n/pdb
• 分子名称: Nephrocystin 1 (1 entity in total)
• 機能のキーワード: beta barrel, cell adhesion
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell junction, adherens junction : O15259
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7623.47

構造登録者

Le Maire, A.,Weber, T.,Saunier, S.,Antignac, C.,Ducruix, A.,Dardel, F. (登録日: 2004-01-07, 公開日: 2005-01-18, 最終更新日: 2024-05-01)

主引用文献

le Maire, A.,Weber, T.,Saunier, S.,Broutin, I.,Antignac, C.,Ducruix, A.,Dardel, F.
Solution NMR structure of the SH3 domain of human nephrocystin and analysis of a mutation-causing juvenile nephronophthisis.
Proteins, 59:347-355, 2005

PubMed Abstract: Human nephrocystin is a protein associated with juvenile NPH, an autosomal recessive, inherited kidney disease responsible for chronic renal failure in children. It contains an SH3 domain involved in signaling pathways controlling cell adhesion and cytoskeleton organization. The solution structure of this domain was solved by triple resonance NMR spectroscopy. Within the core, the structure is similar to those previously reported for other SH3 domains but exhibits a number of specific noncanonical features within the polyproline ligand binding site. Some of the key conserved residues are missing, and the N-Src loop exhibits an unusual twisted geometry, which results in a narrowing of the binding groove. This is induced by the replacement of a conserved Asp, Asn, or Glu residue by a Pro at one side of the N-Src loop. A systematic survey of other SH3 domains also containing a Pro at this position reveals that most of them belong to proteins involved in cell adhesion or motility. A variant of this domain, which carries a point mutation causing NPH, was also analyzed. This change, L180P, although it corresponds to a nonconserved and solvent-exposed position, causes a complete loss of the tertiary structure. Similar effects are also observed with the L180A variant. This could be a context-dependent effect resulting from an interaction between neighboring charged side-chains.

PubMed: 15723349
DOI: 10.1002/prot.20344

実験手法

SOLUTION NMR