1qb2

<table><tr><td colspan='2'>[[1qb2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QB2 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qb2 OCA], [https://pdbe.org/1qb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qb2 RCSB], [https://www.ebi.ac.uk/pdbsum/1qb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qb2 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/SRP54_HUMAN SRP54_HUMAN]] Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein).

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:10497032</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1qb2" style="background-color:#fffaf0;"></div>

*[[Signal recognition particle protein|Signal recognition particle protein]]

[[Category: Human]]

[[Category: Black, S D]]

[[Category: Clemons, W M]]

[[Category: Gowda, K]]

[[Category: Ramakrishnan, V]]

[[Category: Zwieb, C]]

[[Category: Signaling protein]]