2j6f

From Proteopedia

(Difference between revisions)

Current revision

N-TERMINAL SH3 DOMAIN OF CMS (CD2AP HUMAN HOMOLOG) BOUND TO CBL-B PEPTIDE

Structural highlights

2j6f is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.7Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

CD2AP_HUMAN Defects in CD2AP are the cause of susceptibility to focal segmental glomerulosclerosis type 3 (FSGS3) [MIM:607832. A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and edema. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation.^[1]

Function

CD2AP_HUMAN Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton. May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell. May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis.^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The CIN85/CMS (human homologs of mouse SH3KBP1/CD2AP) family of endocytic adaptor proteins has the ability to engage multiple effectors and couple cargo trafficking with the cytoskeleton. CIN85 and CMS (Cas ligand with multiple Src homology 3 (SH3) domains) facilitate the formation of large multiprotein complexes required for an efficient internalization of cell surface receptors. It has recently been shown that c-Cbl/Cbl-b could mediate the formation of a ternary complex between one c-Cbl/Cbl-b molecule and two SH3 domains of CIN85, important for the ability of Cbl to promote epidermal growth factor receptor down-regulation. To further investigate whether multimerization is conserved within the family of adaptor proteins, we have solved the crystal structures of the CMS N-terminal SH3 domain-forming complexes with Cbl-b- and CD2-derived peptides. Together with biochemical evidence, the structures support the notion that, despite clear differences in the interaction surface, both Cbl-b and CD2 can mediate multimerization of N-terminal CMS SH3 domains. Detailed analyses on the interacting surfaces also provide the basis for a differential Cbl-b molecular recognition of CMS and CIN85.

Atypical polyproline recognition by the CMS N-terminal Src homology 3 domain.,Moncalian G, Cardenes N, Deribe YL, Spinola-Amilibia M, Dikic I, Bravo J J Biol Chem. 2006 Dec 15;281(50):38845-53. Epub 2006 Oct 3. PMID:17020880^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kim JM, Wu H, Green G, Winkler CA, Kopp JB, Miner JH, Unanue ER, Shaw AS. CD2-associated protein haploinsufficiency is linked to glomerular disease susceptibility. Science. 2003 May 23;300(5623):1298-300. PMID:12764198 doi:10.1126/science.1081068
↑ Monzo P, Gauthier NC, Keslair F, Loubat A, Field CM, Le Marchand-Brustel Y, Cormont M. Clues to CD2-associated protein involvement in cytokinesis. Mol Biol Cell. 2005 Jun;16(6):2891-902. Epub 2005 Mar 30. PMID:15800069 doi:E04-09-0773
↑ Moncalian G, Cardenes N, Deribe YL, Spinola-Amilibia M, Dikic I, Bravo J. Atypical polyproline recognition by the CMS N-terminal Src homology 3 domain. J Biol Chem. 2006 Dec 15;281(50):38845-53. Epub 2006 Oct 3. PMID:17020880 doi:10.1074/jbc.M606411200

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2j6f"

@@ Line 1: / Line 1: @@
-[[Image:2j6f.gif|left|200px]]<br />
-<applet load="2j6f" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2j6f, resolution 1.697&Aring;" />
-'''N-TERMINAL SH3 DOMAIN OF CMS (CD2AP HUMAN HOMOLOG) BOUND TO CBL-B PEPTIDE'''<br />
-==Overview==
+==N-TERMINAL SH3 DOMAIN OF CMS (CD2AP HUMAN HOMOLOG) BOUND TO CBL-B PEPTIDE==
-The CIN85/CMS (human homologs of mouse SH3KBP1/CD2AP) family of endocytic, adaptor proteins has the ability to engage multiple effectors and couple, cargo trafficking with the cytoskeleton. CIN85 and CMS (Cas ligand with, multiple Src homology 3 (SH3) domains) facilitate the formation of large, multiprotein complexes required for an efficient internalization of cell, surface receptors. It has recently been shown that c-Cbl/Cbl-b could, mediate the formation of a ternary complex between one c-Cbl/Cbl-b, molecule and two SH3 domains of CIN85, important for the ability of Cbl to, promote epidermal growth factor receptor down-regulation. To further, investigate whether multimerization is conserved within the family of, adaptor proteins, we have solved the crystal structures of the CMS, N-terminal SH3 domain-forming complexes with Cbl-b- and CD2-derived, peptides. Together with biochemical evidence, the structures support the, notion that, despite clear differences in the interaction surface, both, Cbl-b and CD2 can mediate multimerization of N-terminal CMS SH3 domains., Detailed analyses on the interacting surfaces also provide the basis for a, differential Cbl-b molecular recognition of CMS and CIN85.
+<StructureSection load='2j6f' size='340' side='right'caption='[[2j6f]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2j6f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J6F FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=2j6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j6f OCA], [https://pdbe.org/2j6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j6f RCSB], [https://www.ebi.ac.uk/pdbsum/2j6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j6f ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/CD2AP_HUMAN CD2AP_HUMAN] Defects in CD2AP are the cause of susceptibility to focal segmental glomerulosclerosis type 3 (FSGS3) [MIM:[https://omim.org/entry/607832 607832]. A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and edema. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation.<ref>PMID:12764198</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/CD2AP_HUMAN CD2AP_HUMAN] Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton. May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell. May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis.<ref>PMID:15800069</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j6/2j6f_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2j6f ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The CIN85/CMS (human homologs of mouse SH3KBP1/CD2AP) family of endocytic adaptor proteins has the ability to engage multiple effectors and couple cargo trafficking with the cytoskeleton. CIN85 and CMS (Cas ligand with multiple Src homology 3 (SH3) domains) facilitate the formation of large multiprotein complexes required for an efficient internalization of cell surface receptors. It has recently been shown that c-Cbl/Cbl-b could mediate the formation of a ternary complex between one c-Cbl/Cbl-b molecule and two SH3 domains of CIN85, important for the ability of Cbl to promote epidermal growth factor receptor down-regulation. To further investigate whether multimerization is conserved within the family of adaptor proteins, we have solved the crystal structures of the CMS N-terminal SH3 domain-forming complexes with Cbl-b- and CD2-derived peptides. Together with biochemical evidence, the structures support the notion that, despite clear differences in the interaction surface, both Cbl-b and CD2 can mediate multimerization of N-terminal CMS SH3 domains. Detailed analyses on the interacting surfaces also provide the basis for a differential Cbl-b molecular recognition of CMS and CIN85.
-==About this Structure==
+Atypical polyproline recognition by the CMS N-terminal Src homology 3 domain.,Moncalian G, Cardenes N, Deribe YL, Spinola-Amilibia M, Dikic I, Bravo J J Biol Chem. 2006 Dec 15;281(50):38845-53. Epub 2006 Oct 3. PMID:17020880<ref>PMID:17020880</ref>
-J6F is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J6F OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Atypical polyproline recognition by the CMS N-terminal Src homology 3 domain., Moncalian G, Cardenes N, Deribe YL, Spinola-Amilibia M, Dikic I, Bravo J, J Biol Chem. 2006 Dec 15;281(50):38845-53. Epub 2006 Oct 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17020880 17020880]
+</div>
-[[Category: Homo sapiens]]
+<div class="pdbe-citations 2j6f" style="background-color:#fffaf0;"></div>
-[[Category: Protein complex]]
-[[Category: Bravo, J.]]
-[[Category: Cardenes, N.]]
-[[Category: Deribe, Y.L.]]
-[[Category: Dikic, I.]]
-[[Category: Moncalian, G.]]
-[[Category: Spinola-Amilibia, M.]]
-[[Category: adaptor protein]]
-[[Category: alternative splicing]]
-[[Category: calcium]]
-[[Category: cd2 associated protein]]
-[[Category: coiled coil]]
-[[Category: cytoskeletal rearrangements]]
-[[Category: egfr downregulation]]
-[[Category: immune response]]
-[[Category: ligase]]
-[[Category: metal-binding]]
-[[Category: phosphorylation]]
-[[Category: polymorphism]]
-[[Category: protein binding]]
-[[Category: sh2 domain]]
-[[Category: sh3]]
-[[Category: sh3 domain]]
-[[Category: sh3-binding]]
-[[Category: ubl conjugation]]
-[[Category: ubl conjugation pathway]]
-[[Category: zinc]]
-[[Category: zinc-finger]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:52:25 2007''
+==See Also==
+*[[CD2-associated protein 3D structures|CD2-associated protein 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Bravo J]]
+[[Category: Cardenes N]]
+[[Category: Deribe YL]]
+[[Category: Dikic I]]
+[[Category: Moncalian G]]
+[[Category: Spinola-Amilibia M]]

2j6f

From Proteopedia

Current revision

N-TERMINAL SH3 DOMAIN OF CMS (CD2AP HUMAN HOMOLOG) BOUND TO CBL-B PEPTIDE

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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