2d10: Difference between revisions

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[[Image:2d10.png|left|200px]]
{{STRUCTURE_2d10|  PDB=2d10  |  SCENE=  }}  
{{STRUCTURE_2d10|  PDB=2d10  |  SCENE=  }}  
===Crystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail peptide===
{{ABSTRACT_PUBMED_16615918}}


===Crystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail peptide===
==Disease==
[[http://www.uniprot.org/uniprot/NHERF_HUMAN NHERF_HUMAN]] Defects in SLC9A3R1 are the cause of hypophosphatemic nephrolithiasis/osteoporosis type 2 (NPHLOP2) [MIM:[http://omim.org/entry/612287 612287]]. Hypophosphatemia results from idiopathic renal phosphate loss. It contributes to the pathogenesis of hypophosphatemic urolithiasis (formation of urinary calculi) as well to that of hypophosphatemic osteoporosis (bone demineralization).<ref>PMID:18784102</ref><ref>PMID:22506049</ref>


{{ABSTRACT_PUBMED_16615918}}
==Function==
[[http://www.uniprot.org/uniprot/RADI_MOUSE RADI_MOUSE]] Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. [[http://www.uniprot.org/uniprot/NHERF_HUMAN NHERF_HUMAN]] Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for recycling of internalized ADRB2. Was first known to play a role in the regulation of the activity and subcellular location of SLC9A3. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May enhance Wnt signaling. May participate in HTR4 targeting to microvilli (By similarity). Involved in the regulation of phosphate reabsorption in the renal proximal tubules.<ref>PMID:9430655</ref><ref>PMID:9096337</ref><ref>PMID:10499588</ref><ref>PMID:18784102</ref>


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:016615918</ref><ref group="xtra">PMID:012499563</ref><ref group="xtra">PMID:010970839</ref><ref group="xtra">PMID:012554651</ref><references group="xtra"/>
<ref group="xtra">PMID:016615918</ref><ref group="xtra">PMID:012499563</ref><ref group="xtra">PMID:010970839</ref><ref group="xtra">PMID:012554651</ref><references group="xtra"/><references/>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Hakoshima, T.]]
[[Category: Hakoshima, T.]]

Revision as of 01:36, 25 March 2013

Template:STRUCTURE 2d10

Crystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail peptideCrystal structure of the Radixin FERM domain complexed with the NHERF-1 C-terminal tail peptide

Template:ABSTRACT PUBMED 16615918

DiseaseDisease

[NHERF_HUMAN] Defects in SLC9A3R1 are the cause of hypophosphatemic nephrolithiasis/osteoporosis type 2 (NPHLOP2) [MIM:612287]. Hypophosphatemia results from idiopathic renal phosphate loss. It contributes to the pathogenesis of hypophosphatemic urolithiasis (formation of urinary calculi) as well to that of hypophosphatemic osteoporosis (bone demineralization).[1][2]

FunctionFunction

[RADI_MOUSE] Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. [NHERF_HUMAN] Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for recycling of internalized ADRB2. Was first known to play a role in the regulation of the activity and subcellular location of SLC9A3. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May enhance Wnt signaling. May participate in HTR4 targeting to microvilli (By similarity). Involved in the regulation of phosphate reabsorption in the renal proximal tubules.[3][4][5][6]

About this StructureAbout this Structure

2d10 is a 8 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1][xtra 2][xtra 3][xtra 4]

  1. ↑ Terawaki S, Maesaki R, Hakoshima T. Structural basis for NHERF recognition by ERM proteins. Structure. 2006 Apr;14(4):777-89. PMID:16615918 doi:10.1016/j.str.2006.01.015
  2. ↑ Terawaki S, Maesaki R, Okada K, Hakoshima T. Crystallographic characterization of the radixin FERM domain bound to the C-terminal region of the human Na+/H+-exchanger regulatory factor (NHERF). Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):177-9. Epub 2002, Dec 19. PMID:12499563
  3. ↑ Hamada K, Shimizu T, Matsui T, Tsukita S, Hakoshima T. Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J. 2000 Sep 1;19(17):4449-62. PMID:10970839 doi:10.1093/emboj/19.17.4449
  4. ↑ Hamada K, Shimizu T, Yonemura S, Tsukita S, Tsukita S, Hakoshima T. Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex. EMBO J. 2003 Feb 3;22(3):502-14. PMID:12554651 doi:10.1093/emboj/cdg039
  1. ↑ Karim Z, Gerard B, Bakouh N, Alili R, Leroy C, Beck L, Silve C, Planelles G, Urena-Torres P, Grandchamp B, Friedlander G, Prie D. NHERF1 mutations and responsiveness of renal parathyroid hormone. N Engl J Med. 2008 Sep 11;359(11):1128-35. PMID:18784102 doi:359/11/1128
  2. ↑ Courbebaisse M, Leroy C, Bakouh N, Salaun C, Beck L, Grandchamp B, Planelles G, Hall RA, Friedlander G, Prie D. A new human NHERF1 mutation decreases renal phosphate transporter NPT2a expression by a PTH-independent mechanism. PLoS One. 2012;7(4):e34764. doi: 10.1371/journal.pone.0034764. Epub 2012 Apr 10. PMID:22506049 doi:10.1371/journal.pone.0034764
  3. ↑ Murthy A, Gonzalez-Agosti C, Cordero E, Pinney D, Candia C, Solomon F, Gusella J, Ramesh V. NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins. J Biol Chem. 1998 Jan 16;273(3):1273-6. PMID:9430655
  4. ↑ Yun CH, Oh S, Zizak M, Steplock D, Tsao S, Tse CM, Weinman EJ, Donowitz M. cAMP-mediated inhibition of the epithelial brush border Na+/H+ exchanger, NHE3, requires an associated regulatory protein. Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):3010-5. PMID:9096337
  5. ↑ Cao TT, Deacon HW, Reczek D, Bretscher A, von Zastrow M. A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor. Nature. 1999 Sep 16;401(6750):286-90. PMID:10499588 doi:10.1038/45816
  6. ↑ Karim Z, Gerard B, Bakouh N, Alili R, Leroy C, Beck L, Silve C, Planelles G, Urena-Torres P, Grandchamp B, Friedlander G, Prie D. NHERF1 mutations and responsiveness of renal parathyroid hormone. N Engl J Med. 2008 Sep 11;359(11):1128-35. PMID:18784102 doi:359/11/1128

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