HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Takai, Y. Articles by Hakoshima, T. Search for Related Content PubMed Articles by Takai, Y. Articles by Hakoshima, T.

¹ Structural Biology Laboratory, Nara Institute of Science and Technology, and
² CREST, Japan Science and Technology Agency, 8916-5, Takayama, Ikoma, Nara 630-0192, Japan

P-selectin glycoprotein ligand-1 (PSGL-1), an adhesion molecule with O-glycosylated extracellular sialomucins, is involved in leukocyte inflammatory responses. On activation, ezrin–radixin–moesin (ERM) proteins mediate the redistribution of PSGL-1 on polarized cell surfaces to facilitate binding to target molecules. ERM proteins recognize a short binding motif, Motif-1, conserved in cytoplasmic tails of adhesion molecules, whereas PSGL-1 lacks Motif-1 residues important for binding to ERM proteins. The crystal structure of the complex between the radixin FERM domain and a PSGL-1 juxtamembrane peptide reveals that the peptide binds the groove of FERM subdomain C by forming a β-strand associated with strand β5C, followed by a loop flipped out towards the solvent. The Motif-1 3₁₀ helix present in the FERM–ICAM-2 complex is absent in PSGL-1 given the absence of a critical Motif-1 alanine residue, and PSGL-1 reduces its contact area with subdomain C. Non-conserved positions are occupied by large residues Met9 and His8, which stabilize peptide conformation and enhance groove binding. Non-conserved residues play an important role in compensating for loss of binding energy resulting from the absence of conserved residues important for binding.

^* Correspondence: E-mail: hakosima{at}bs.naist.jp

This article has been cited by other articles:

				A. Zarbock, H. Muller, Y. Kuwano, and K. Ley PSGL-1-dependent myeloid leukocyte activation J. Leukoc. Biol., November 1, 2009; 86(5): 1119 - 1124. [Abstract] [Full Text] [PDF]

				D. J. Killock, M. Parsons, M. Zarrouk, S. M. Ameer-Beg, A. J. Ridley, D. O. Haskard, M. Zvelebil, and A. Ivetic In Vitro and in Vivo Characterization of Molecular Interactions between Calmodulin, Ezrin/Radixin/Moesin, and L-selectin J. Biol. Chem., March 27, 2009; 284(13): 8833 - 8845. [Abstract] [Full Text] [PDF]

				T. Mori, K. Kitano, S.-i. Terawaki, R. Maesaki, Y. Fukami, and T. Hakoshima Structural Basis for CD44 Recognition by ERM Proteins J. Biol. Chem., October 24, 2008; 283(43): 29602 - 29612. [Abstract] [Full Text] [PDF]

				J. J. Miner, L. Xia, T. Yago, J. Kappelmayer, Z. Liu, A. G. Klopocki, B. Shao, J. M. McDaniel, H. Setiadi, D. W. Schmidtke, et al. Separable requirements for cytoplasmic domain of PSGL-1 in leukocyte rolling and signaling under flow Blood, September 1, 2008; 112(5): 2035 - 2045. [Abstract] [Full Text] [PDF]