1qb2
From Proteopedia
(New page: 200px<br /> <applet load="1qb2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qb2, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1qb2. | + | [[Image:1qb2.jpg|left|200px]]<br /><applet load="1qb2" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1qb2" size=" | + | |
caption="1qb2, resolution 2.1Å" /> | caption="1qb2, resolution 2.1Å" /> | ||
'''CRYSTAL STRUCTURE OF THE CONSERVED SUBDOMAIN OF HUMAN PROTEIN SRP54M AT 2.1A RESOLUTION: EVIDENCE FOR THE MECHANISM OF SIGNAL PEPTIDE BINDING'''<br /> | '''CRYSTAL STRUCTURE OF THE CONSERVED SUBDOMAIN OF HUMAN PROTEIN SRP54M AT 2.1A RESOLUTION: EVIDENCE FOR THE MECHANISM OF SIGNAL PEPTIDE BINDING'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1QB2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1QB2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QB2 OCA]. |
==Reference== | ==Reference== | ||
| Line 22: | Line 21: | ||
[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:43:44 2008'' |
Revision as of 14:43, 15 February 2008
|
CRYSTAL STRUCTURE OF THE CONSERVED SUBDOMAIN OF HUMAN PROTEIN SRP54M AT 2.1A RESOLUTION: EVIDENCE FOR THE MECHANISM OF SIGNAL PEPTIDE BINDING
Overview
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.
About this Structure
1QB2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the conserved subdomain of human protein SRP54M at 2.1 A resolution: evidence for the mechanism of signal peptide binding., Clemons WM Jr, Gowda K, Black SD, Zwieb C, Ramakrishnan V, J Mol Biol. 1999 Sep 24;292(3):697-705. PMID:10497032
Page seeded by OCA on Fri Feb 15 16:43:44 2008
