1ri9

From Proteopedia

(Difference between revisions)

Revision as of 08:24, 14 June 2023

Structure of a helically extended SH3 domain of the T cell adapter protein ADAP

Structural highlights

1ri9 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

FYB1_HUMAN Congenital autosomal recessive small-platelet thrombocytopenia. The disease is caused by variants affecting the gene represented in this entry.

Function

FYB1_HUMAN Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells (By similarity). May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (PubMed:10747096, PubMed:16980616). Modulates the expression of IL2 (By similarity). Involved in platelet activation (By similarity). Prevents the degradation of SKAP1 and SKAP2 (PubMed:15849195). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells (By similarity).[UniProtKB:D3ZIE4][UniProtKB:O35601]^[1] ^[2] ^[3]

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 adapter protein ADAP (FYB/SLAP-130) provides a critical link between T cell receptor (TCR) signaling and cell adhesion via the activation of integrins. The C-terminal 70 residues of ADAP show homology to SH3 domains; however, conserved residues of the fold are absent. An alignment and annotation of this domain has therefore been elusive. We have solved the three-dimensional structure of the ADAP C-terminal domain by NMR spectroscopy and show that it represents an altered SH3 domain fold. An N-terminal, amphipathic helix makes extensive contacts to residues of the regular SH3 domain fold, and thereby a composite surface with unusual surface properties is created. We propose this SH3 domain variant to be classified as a helically extended SH3 domain (hSH3 domain) and show that the ADAP-hSH3 domain can no longer bind conventional proline-rich peptides.

Structure of a helically extended SH3 domain of the T cell adapter protein ADAP.,Heuer K, Kofler M, Langdon G, Thiemke K, Freund C Structure. 2004 Apr;12(4):603-10. PMID:15062083^[4]

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

References

↑ Krause M, Sechi AS, Konradt M, Monner D, Gertler FB, Wehland J. Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton. J Cell Biol. 2000 Apr 3;149(1):181-94. PMID:10747096
↑ Huang Y, Norton DD, Precht P, Martindale JL, Burkhardt JK, Wange RL. Deficiency of ADAP/Fyb/SLAP-130 destabilizes SKAP55 in Jurkat T cells. J Biol Chem. 2005 Jun 24;280(25):23576-83. Epub 2005 Apr 22. PMID:15849195 doi:http://dx.doi.org/10.1074/jbc.M413201200
↑ Kliche S, Breitling D, Togni M, Pusch R, Heuer K, Wang X, Freund C, Kasirer-Friede A, Menasche G, Koretzky GA, Schraven B. The ADAP/SKAP55 signaling module regulates T-cell receptor-mediated integrin activation through plasma membrane targeting of Rap1. Mol Cell Biol. 2006 Oct;26(19):7130-44. PMID:16980616 doi:http://dx.doi.org/26/19/7130
↑ Heuer K, Kofler M, Langdon G, Thiemke K, Freund C. Structure of a helically extended SH3 domain of the T cell adapter protein ADAP. Structure. 2004 Apr;12(4):603-10. PMID:15062083 doi:10.1016/j.str.2004.02.021

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ri9"

@@ Line 1: / Line 1: @@
 ==Structure of a helically extended SH3 domain of the T cell adapter protein ADAP==
-<StructureSection load='1ri9' size='340' side='right'caption='[[1ri9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1ri9' size='340' side='right'caption='[[1ri9]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ri9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RI9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ri9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RI9 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FYB, SLAP130 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</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=1ri9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ri9 OCA], [https://pdbe.org/1ri9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ri9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ri9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ri9 ProSAT]</span></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=1ri9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ri9 OCA], [https://pdbe.org/1ri9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ri9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ri9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ri9 ProSAT]</span></td></tr>
 </table>
+== Disease ==
+[https://www.uniprot.org/uniprot/FYB1_HUMAN FYB1_HUMAN] Congenital autosomal recessive small-platelet thrombocytopenia. The disease is caused by variants affecting the gene represented in this entry.
 == Function ==
-[[https://www.uniprot.org/uniprot/FYB_HUMAN FYB_HUMAN]] Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells. Modulates the expression of interleukin-2 (IL-2). Involved in platelet activation. Prevents the degradation of SKAP1 and SKAP2. May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton.<ref>PMID:10747096</ref> <ref>PMID:15849195</ref> <ref>PMID:16980616</ref>
+[https://www.uniprot.org/uniprot/FYB1_HUMAN FYB1_HUMAN] Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells (By similarity). May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (PubMed:10747096, PubMed:16980616). Modulates the expression of IL2 (By similarity). Involved in platelet activation (By similarity). Prevents the degradation of SKAP1 and SKAP2 (PubMed:15849195). May be involved in high affinity immunoglobulin epsilon receptor signaling in mast cells (By similarity).[UniProtKB:D3ZIE4][UniProtKB:O35601]<ref>PMID:10747096</ref> <ref>PMID:15849195</ref> <ref>PMID:16980616</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Freund, C]]
+[[Category: Freund C]]
-[[Category: Heuer, K]]
+[[Category: Heuer K]]
-[[Category: Kofler, M]]
+[[Category: Kofler M]]
-[[Category: Langdon, G]]
+[[Category: Langdon G]]
-[[Category: Thiemke, K]]
+[[Category: Thiemke K]]
-[[Category: Helically extended]]
-[[Category: Sh3-like]]
-[[Category: Signaling protein]]

1ri9

From Proteopedia

Revision as of 08:24, 14 June 2023

Structure of a helically extended SH3 domain of the T cell adapter protein ADAP

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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