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1ywi

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Revision as of 16:47, 29 January 2020

Structure of the FBP11WW1 domain complexed to the peptide APPTPPPLPP

Structural highlights

1ywi is a 2 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1f8a, 1i5h, 1eg4, 1cka, 1o6w, 1ywj
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PR40A_HUMAN] Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.^[1]

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

WW domains are small protein-protein interaction modules that recognize proline-rich stretches in proteins. The class II tandem WW domains of the formin binding protein 11 (FBP11) recognize specifically proteins containing PPLPp motifs as present in the formins that are involved in limb and kidney development, and in the methyl-CpG-binding protein 2 (MeCP2), associated with the Rett syndrome. The interaction involves the specific recognition of a leucine side-chain. Here, we report on the novel structure of the complex formed by the FPB11WW1 domain and the formin fragment APPTPPPLPP revealing the specificity determinants of class II WW domains.

Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain.,Pires JR, Parthier C, Aido-Machado R, Wiedemann U, Otte L, Bohm G, Rudolph R, Oschkinat H J Mol Biol. 2005 Apr 29;348(2):399-408. PMID:15811376^[2]

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

References

↑ Bai SW, Herrera-Abreu MT, Rohn JL, Racine V, Tajadura V, Suryavanshi N, Bechtel S, Wiemann S, Baum B, Ridley AJ. Identification and characterization of a set of conserved and new regulators of cytoskeletal organization, cell morphology and migration. BMC Biol. 2011 Aug 11;9:54. doi: 10.1186/1741-7007-9-54. PMID:21834987 doi:10.1186/1741-7007-9-54
↑ Pires JR, Parthier C, Aido-Machado R, Wiedemann U, Otte L, Bohm G, Rudolph R, Oschkinat H. Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain. J Mol Biol. 2005 Apr 29;348(2):399-408. PMID:15811376 doi:http://dx.doi.org/10.1016/j.jmb.2005.02.056

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Structure of the FBP11WW1 domain complexed to the peptide APPTPPPLPP==
-<StructureSection load='1ywi' size='340' side='right' caption='[[1ywi]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
+<StructureSection load='1ywi' size='340' side='right'caption='[[1ywi]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1ywi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YWI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YWI FirstGlance]. <br>
@@ Line 33: / Line 33: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Aido-Machado, R]]
 [[Category: Boehm, G]]

1ywi

From Proteopedia

Revision as of 16:47, 29 January 2020

Structure of the FBP11WW1 domain complexed to the peptide APPTPPPLPP

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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