1QB2
CRYSTAL STRUCTURE OF THE CONSERVED SUBDOMAIN OF HUMAN PROTEIN SRP54M AT 2.1A RESOLUTION: EVIDENCE FOR THE MECHANISM OF SIGNAL PEPTIDE BINDING
1QB2 の概要
エントリーDOI | 10.2210/pdb1qb2/pdb |
分子名称 | HUMAN SIGNAL RECOGNITION PARTICLE 54 KD PROTEIN (2 entities in total) |
機能のキーワード | alpha-helix, helix-turn-helix, signaling protein |
由来する生物種 | Homo sapiens (human) |
細胞内の位置 | Nucleus speckle : P61011 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 24946.88 |
構造登録者 | Clemons Jr., W.M.,Gowda, K.,Black, S.D.,Zwieb, C.,Ramakrishnan, V. (登録日: 1999-04-29, 公開日: 1999-10-20, 最終更新日: 2024-02-14) |
主引用文献 | Clemons Jr., W.M.,Gowda, K.,Black, S.D.,Zwieb, C.,Ramakrishnan, V. Crystal structure of the conserved subdomain of human protein SRP54M at 2.1 A resolution: evidence for the mechanism of signal peptide binding. J.Mol.Biol., 292:697-705, 1999 Cited by PubMed Abstract: Protein SRP54 is an integral part of the mammalian signal recognition particle (SRP), a cytosolic ribonucleoprotein complex which associates with ribosomes and serves to recognize, bind, and transport proteins destined for the membrane or secretion. The methionine-rich M-domain of protein SRP54 (SRP54M) binds the SRP RNA and the signal peptide as the nascent protein emerges from the ribosome. A focal point of this critical cellular function is the detailed understanding of how different hydrophobic signal peptides are recognized efficiently and transported specifically, despite considerable variation in sequence. We have solved the crystal structure of a conserved functional subdomain of the human SRP54 protein (hSRP54m) at 2.1 A resolution showing a predominantly alpha helical protein with a large fraction of the structure available for binding. RNA binding is predicted to occur in the vicinity of helices 4 to 6. The N-terminal helix extends significantly from the core of the structure into a large but constricted hydrophobic groove of an adjacent molecule, thus revealing molecular details of possible interactions between alpha helical signal peptides and human SRP54. PubMed: 10497032DOI: 10.1006/jmbi.1999.3090 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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