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首页> 美国卫生研究院文献>BMC Evolutionary Biology >The origins and developments of sulfation-prone tyrosine-rich and acidic N- and C-terminal extensions of class ll and lll small leucine-rich repeat proteins shed light on connective tissue evolution in vertebrates
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The origins and developments of sulfation-prone tyrosine-rich and acidic N- and C-terminal extensions of class ll and lll small leucine-rich repeat proteins shed light on connective tissue evolution in vertebrates

机译：硫化型富毒素的富含酪氨​​酸富含和酸性N-和C末端延伸的起源和发展以及LL和LLL小亮氨酸的富含蛋白质缩小的脊椎动物的结缔组织演化

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Phylogenetic analysis of human SLRPs and schematic representation of class II and III SLRPs. a The rooted dendrogram shows the phylogenetic relationship between the 18 known human SLRPs with colours displaying the five classes of SLRPs. b Crystal structure of fibromodulin (PDB: 5MX0). Open-Source PyMOL was used for presenting the crystal structure. The fibromodulin structure contains several sugar moieties (dark green) and three disulfide-bridges formed between cysteine residues (yellow) in the N- and C-terminal cysteine motifs. The N-terminus is pointing upwards. Note that the variable N-terminal region of fibromodulin is not visible in the structure due to its disordered structure. The leucine-rich repeat consensus sequence (LXXLXLXXNXL, where L is leucine or another hydrophobic residue, N is asparagine and X is any residue) is shown. The repetition of this motif gives the SLRPs their topology with parallel β-strands on the inner concave face and a variable structure on the outer convex face resulting in an overall curved solenoid structure. c Schematic representation of selected elements in the terminal regions of human class II and III SLRPs. The dots in the dashed lines represent leucine-rich repeats, while solid lines represent the N- and C-terminal regions of the SLRPs. Yellow lines represent termini experimentally known to be sulfated, while the green lines represent termini predicted to be sulfated according to current literature. The letter abbreviations denote the following features: “pQ” indicates an N-terminal glutamine which in vivo will cyclize into pyroglutamate (pQ); “Y” represent tyrosines; “sY” are tyrosine sites for which sulfation has been identified experimentally in humans; “D” and “E” represent the aspartic and glutamic acid residues clustered in the C-terminal region of osteoadherin; “P” and “R” represent the prolines and arginines in the N-terminal region of PRELP
机译：人物SLRP的系统发育分析及II类和III SLRPS的示意图。生根的树枝图显示了18个已知的人SLRPS之间的系统发育关系，颜色显示出五类SLRPS。 B纤维苷晶体结构（PDB：5MX0）。使用开源pymol用于呈现晶体结构。纤维蛋白结构含有几种糖部分（深绿色）和三种在半胱氨酸残基（黄色）之间形成的三种二硫桥，在N-和C-末端半胱氨酸基序中形成。 n-terminus是向上指向的。注意，由于其无序结构，在结构中不可见纤维蛋白的可变N-末端区域。富含亮氨酸的重复共有序列（LXXLXLXNX1，其中L是亮氨酸或另一种疏水残留物，N是天冬酰胺，X是任何残留物）。该基序的重复使SLRPS在内部凹面上的平行β-股线和外部凸面上的可变结构，导致整体弯曲螺线管结构。 C人类II和III SLRPS终端区域中所选元素的C示意图。虚线中的点代表富含亮氨酸的重复，而实线代表SLRPS的N-和C末端区域。黄线代表实验硫化的Termini，而绿线代表Termini预测根据当前文献硫化。字母缩写表示以下特征：“PQ”表示在体内的N-末端谷氨酰胺将环形为吡酰磺酸盐（PQ）; “Y”代表酪氨酸; “sy”是酪氨酸位点，用于在人类中实验鉴定硫酸盐; “D”和“E”代表在骨蛋白的C末端区域聚集的天冬氨酸和谷氨酸残基; “P”和“R”代表PRELP的N末端区域中的脯氨酸和精氨酸

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