2hac
From Proteopedia
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'''Structure of Zeta-Zeta Transmembrane Dimer''' | '''Structure of Zeta-Zeta Transmembrane Dimer''' | ||
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[[Category: Schnell, J R.]] | [[Category: Schnell, J R.]] | ||
[[Category: Wucherpfennig, K W.]] | [[Category: Wucherpfennig, K W.]] | ||
| - | [[Category: | + | [[Category: Alpha helix]] |
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:03:03 2008'' | |
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Revision as of 03:03, 4 May 2008
Structure of Zeta-Zeta Transmembrane Dimer
Overview
The T cell receptor (TCR) alphabeta heterodimer communicates ligand binding to the cell interior via noncovalently associated CD3gammaepsilon, CD3deltaepsilon, and zetazeta dimers. While structures of extracellular components of the TCR-CD3 complex are known, the transmembrane (TM) domains that mediate assembly have eluded structural characterization. Incorporation of the zetazeta signaling module is known to require one basic TCRalpha and two zetazeta aspartic acid TM residues. We report the NMR structure of the zetazeta(TM) dimer, a left-handed coiled coil with substantial polar contacts. Mutagenesis experiments demonstrate that three polar positions are critical for zetazeta dimerization and assembly with TCR. The two aspartic acids create a single structural unit at the zetazeta interface stabilized by extensive hydrogen bonding, and there is evidence for a structural water molecule (or molecules) within close proximity. This structural unit, representing only the second transmembrane dimer interface solved to date, serves as a paradigm for the assembly of all modules involved in TCR signaling.
About this Structure
2HAC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of the zetazeta transmembrane dimer reveals features essential for its assembly with the T cell receptor., Call ME, Schnell JR, Xu C, Lutz RA, Chou JJ, Wucherpfennig KW, Cell. 2006 Oct 20;127(2):355-68. PMID:17055436 Page seeded by OCA on Sun May 4 06:03:03 2008
