WW domains Structure Volume 4, Issue 5, Pages (May 1996)

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WW domains Structure Volume 4, Issue 5, Pages 495-499 (May 1996) Olivier Staub, Daniela Rotin Structure Volume 4, Issue 5, Pages 495-499 (May 1996) DOI: 10.1016/S0969-2126(96)00054-8

Figure 1 Schematic representation of several proteins containing WW domains (red). A single boxed W (e.g. in DP71 and K01A6.1) represents a portion of the domain containing either the first or second conserved tryptophan. The C2 domain (a domain known to mediate Ca2+-dependent association with phospholipids/membranes) is found in Nedd4/Rsp5 and also in PKC, PLA2, PLC, rasGAP, synaptotagmin I and other proteins. The HECT domain in Nedd4/Rsp5 and 56G7 is a ubiquitin ligase (E3) enzyme also present in E6-AP, the yeast ykl162, rat p 100 and UreB1. Pro represents the proline-rich (SH3 binding) region; Cys, cysteine rich region; TM, transmembrane domain of CD45 associated protein (CD45AP); PH, pleckstrin homology domain also found in dynamin, SOS, PLCγ, IRS-1, rasGAP and Btk; BCR (breakpoint cluster region) homology domain, also shared by p85 of PI-3 kinase, rhoGAP and n-chimerin; PTB/PID domains, recently suggested to be a subclass of PH domains, are also present in Shc, numb and IRS-1; PPlase, peptidylpropyl cis-trans isomerase, known to associate with transcription factors; PTP, homologous to protein tyrosine phosphatases. Actin binding (CH, calponin homology) domain is homologous to calponin, actinin, vav and spectrin. In human ORF1 (IQGAP1), the Mp domain is homologous to the fly muscle protein mp20, and the GTPase activator is a rasGAP domain. The Y domain, shared by Yo61 and Ykb2, has no known function. Sizes of all proteins and domains are not to scale. Structure 1996 4, 495-499DOI: (10.1016/S0969-2126(96)00054-8)

Figure 2 Sequence alignment of WW domains from different proteins and the suggested WW consensus sequence. Invariant residues are in bold letters. Conserved residues in the consensus sequence are in capital letters; h represents hydrophobic residues; t corresponds to polar or charged (turn-like) residues. Boxes under the consensus sequence indicate location of the β1, β2, and β3 strands of the WW domain, determined by H Oschkinat and colleagues (H Oschkinat, personal communication). Sequences shown at the bottom of the figure are of putative WW domains in which not all of the invariant amino acids are conserved, or the domain is split in two. Dots represent spaces introduced to maximize homology. Dashes (in DP71) represent an unrelated amino acid sequence. In the formin-binding proteins FBP11, 21, 23, 28 and 30, sequences surrounding the indicated amino acids [13] have not been provided. Structure 1996 4, 495-499DOI: (10.1016/S0969-2126(96)00054-8)