I-domain

Fig. 11.4 The dependence of P, (PeL) and q, (PeL). The dotted line shows Pol = Peer I domain PeL < Peer, II domain Pcl > Peer, I critical point, 2 qt = 0. Reprinted from Hetsroni et al. (2004) with permission...

SWi, which in turn is related to the homonuclear or heteronuclear coupling constants. In homonuclear 2D spectra, the transmitter offset frequency is kept at the center of (i.e., at = 0) and F domains. In heteronuclear-shift-correlated spectra, the decoupler offset frequency is kept at the center (Fi = 0) of thei i domain, with the domain corresponding to the invisible or decoupled nucleus. 

In the i-domain, convolution is simply the product of the Laplace transform ... 

Fig. 10.3. H sIVU complex. Originally reported (A) and physiologically relevant (B) docking mode between HsIV and HsIU. In the physiologically relevant docking mode, the I-domains of HsIU point away from the HsIV.

H. S., and McKay, D. B. Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome. /. Mol. Biol. 2003, 330, 185-195. 

In potato pectic polysaccharides, the RG-I domain accounts for 75% of the total, a much higher proportion than in pectic polysaccharides of other species ( 20-35%) (Oomen et al., 2003 Mohnen et al., 2008). RG-1 consists of a backbone of alternating a-D-galacturonic acid and a-L-rhamnosyl residues, linked as indicated in Figure 3.3, which in potato accounts for 14% of the total RG-1 (Oomen et al., 2003). Although the galacturonic acid residues are probably not methyl-esterified, they may be acetylated. This is so in potato, where a preparation... 

Fig. 7. Structure of the integrin I domain bound to the IBP triple-helix peptide.

F. Structure of the Headpiece in Integrins that Lack I Domains. 37... 

Fig. 1. Integrin a- and /5-subunits form 24 heterodimers that recognize distinct but overlapping ligands. Half of the a subunits contain I domains (asterisks).

Fig. 2. Integrin architecture. (A) Organization of domains within the primary structure. Some a subunits contain an I domain inserted in the position denoted by the dotted lines. Cysteines and disulfide bonds are shown as lines below the stick figures. Red and blue asterisks denote and Mg " " binding sites, respectively.

B) Arrangement of domains within the three-dimensional crystal structure of (Xiong et al, 2001). Each domain is color coded as in A. (C) The structure in (B) with an I domain added. (See Color Insert.)... 

All integrin (3 subunits and half of integrin a subunits contain von Willebrand factor-type A domains of about 200 amino acids, also referred to as the inserted (I) domain in the a-subunit and the I-like domain in the / subunit, respectively (Figs. 1, 2) (Humphries, 2000 Shimaoka et al,... 

The j3 subunit I-like domain, which is inserted in the hybrid domain of the /3-subunit (Fig. 2A), directly binds ligand in integrins that lack I domains in the a subunit (Fig. 3C, Fig. 6A). By contrast, when the I... 

Fig. 3. Conformational states for integrins. A-C. Model for a l3 integrin activation, with at least three conformations of the extracellular domain (Takagi et al, 2002). (A) Bent, low affinity conformation. (B) Extended conformation with closed headpiece. (C) Extended conformation with open headpiece shown with bound RGD-mimetic peptide (green CPK). D-H. Model for aiJ3 integrin activation. (D) Bent conformation with low affinity. (E) and (F) with a closed headpiece and closed I domain in...

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