2JTE
Third SH3 domain of CD2AP
2JTE の概要
エントリーDOI | 10.2210/pdb2jte/pdb |
NMR情報 | BMRB: 15407 |
分子名称 | CD2-associated protein (1 entity in total) |
機能のキーワード | protein, sh3 domain, coiled coil, cytoplasm, phosphorylation, sh3-binding, signaling protein |
由来する生物種 | Mus musculus (house mouse) |
細胞内の位置 | Cytoplasm, cytoskeleton: Q9JLQ0 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 7146.91 |
構造登録者 | van Nuland, N.A.J.,Ortega, R.J.,Romero Romero, M.,Ab, E.,Ora, A.,Lopez, M.O.,Azuaga, A.I. (登録日: 2007-07-28, 公開日: 2007-12-11, 最終更新日: 2024-05-29) |
主引用文献 | Ortega Roldan, J.L.,Romero Romero, M.L.,Ora, A.,Ab, E.,Lopez Mayorga, O.,Azuaga, A.I.,van Nuland, N.A. The high resolution NMR structure of the third SH3 domain of CD2AP. J.Biomol.Nmr, 39:331-336, 2007 Cited by PubMed Abstract: CD2 associated protein (CD2AP) is an adaptor protein that plays an important role in cell to cell union needed for the kidney function. CD2AP interacts, as an adaptor protein, with different natural targets, such as CD2, nefrin, c-Cbl and podocin. These proteins are believed to interact to one of the three SH3 domains that are positioned in the N-terminal region of CD2AP. To understand the network of interactions between the natural targets and the three SH3 domains (SH3-A, B and C), we have started to determine the structures of the individual SH3 domains. Here we present the high-resolution structure of the SH3-C domain derived from NMR data. Full backbone and side-chain assignments were obtained from triple-resonance spectra. The structure was determined from distance restraints derived from high-resolution 600 and 800 MHz NOESY spectra, together with phi and psi torsion angle restraints based on the analysis of 1HN, 15N, 1Halpha, 13Calpha, 13CO and 13Cbeta chemical shifts. Structures were calculated using CYANA and refined in water using RECOORD. The three-dimensional structure of CD2AP SH3-C contains all the features that are typically found in other SH3 domains, including the general binding site for the recognition of polyproline sequences. PubMed: 17922258DOI: 10.1007/s10858-007-9201-7 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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