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Crystal structure of bovine trypsinogen at 1-8 A resolution. I. Data collection, application of patterson search techniques and preliminary structural interpretation.

作者信息

Bode W, Fehlhammer H, Huber R

出版信息

J Mol Biol. 1976 Sep 15;106(2):325-35. doi: 10.1016/0022-2836(76)90089-9.

DOI:10.1016/0022-2836(76)90089-9
PMID:978726
Abstract
摘要

相似文献

1
Crystal structure of bovine trypsinogen at 1-8 A resolution. I. Data collection, application of patterson search techniques and preliminary structural interpretation.
J Mol Biol. 1976 Sep 15;106(2):325-35. doi: 10.1016/0022-2836(76)90089-9.
2
The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. I. Crystallization, data collection and application of patterson search technique.
J Mol Biol. 1975 Nov 15;98(4):683-92. doi: 10.1016/s0022-2836(75)80004-0.
3
Structure of bovine trypsinogen at 1.9 A resolution.分辨率为1.9埃的牛胰蛋白酶原结构。
Biochemistry. 1977 Feb 22;16(4):654-64. doi: 10.1021/bi00623a016.
4
Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 A resolution. Structure solution, crystallographic refinement and preliminary structural interpretation.分辨率为1.8埃时，胰腺分泌型胰蛋白酶抑制剂（卡扎尔型）与胰蛋白酶原复合物的三维结构。结构解析、晶体学精修及初步结构阐释。
J Mol Biol. 1982 Dec 25;162(4):839-68. doi: 10.1016/0022-2836(82)90550-2.
5
The crystal structure of phosphorylase beta at 6 A resolution.
J Mol Biol. 1974 Dec 25;90(4):703-17. doi: 10.1016/0022-2836(74)90534-8.
6
Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin.通过与胰蛋白酶N端序列相似的肽诱导牛胰蛋白酶原向胰蛋白酶的转变。
FEBS Lett. 1976 Oct 1;68(2):231-6. doi: 10.1016/0014-5793(76)80443-7.
7
The refined 2.2-A (0.22-nm) X-ray crystal structure of the ternary complex formed by bovine trypsinogen, valine-valine and the Arg15 analogue of bovine pancreatic trypsin inhibitor.
Eur J Biochem. 1984 Oct 1;144(1):185-90. doi: 10.1111/j.1432-1033.1984.tb08447.x.
8
The structure of triclinic lysozyme at 2-5 A resolution.分辨率为2-5埃的三斜晶系溶菌酶结构。
J Mol Biol. 1976 Jan 15;100(2):179-95. doi: 10.1016/s0022-2836(76)80147-7.
9
Comparison of various molecular forms of bovine trypsin: correlation of infrared spectra with X-ray crystal structures.牛胰蛋白酶不同分子形式的比较：红外光谱与X射线晶体结构的相关性
Biochemistry. 1991 Jan 8;30(1):133-43. doi: 10.1021/bi00215a020.
10
Preliminary crystallographic data for the structure of the complex between Kazal trypsin inhibitor and trypsinogen.Kazal型胰蛋白酶抑制剂与胰蛋白酶原复合物结构的初步晶体学数据。
J Mol Biol. 1981 Jan 25;145(3):603-5. doi: 10.1016/0022-2836(81)90547-7.

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Pseudotrypsin: A Little-Known Trypsin Proteoform.假性胰蛋白酶：一种鲜为人知的胰蛋白酶蛋白形式。
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Methods of probing the interactions between small molecules and disordered proteins.探究小分子与无序蛋白质之间相互作用的方法。
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Cathepsin L inactivates human trypsinogen, whereas cathepsin L-deletion reduces the severity of pancreatitis in mice.组织蛋白酶 L 可使人类胰蛋白酶原失活，而组织蛋白酶 L 缺失可降低小鼠胰腺炎的严重程度。
Gastroenterology. 2010 Feb;138(2):726-37. doi: 10.1053/j.gastro.2009.10.048. Epub 2009 Nov 10.
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Cathepsin B cleavage of the trypsinogen activation peptide.组织蛋白酶B对胰蛋白酶原激活肽的切割
BMC Gastroenterol. 2002 Jun 27;2:16. doi: 10.1186/1471-230x-2-16.
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The structure of the human betaII-tryptase tetramer: fo(u)r better or worse.人βII-类胰蛋白酶四聚体的结构：无论好坏，皆为四个。
Proc Natl Acad Sci U S A. 1999 Sep 28;96(20):10984-91. doi: 10.1073/pnas.96.20.10984.
8
Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D.前因子D激活的结构基础：从高度灵活的酶原到新型自身抑制性丝氨酸蛋白酶——补体因子D
EMBO J. 1999 Feb 15;18(4):804-14. doi: 10.1093/emboj/18.4.804.
9
Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray crystal structure of single-chain human tPA.赖氨酸156促进组织型纤溶酶原激活剂（tPA）的异常酶原活性：单链人组织型纤溶酶原激活剂的X射线晶体结构
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10
Prediction of the three-dimensional structures of the nerve growth factor and epidermal growth factor binding proteins (kallikreins) and an hypothetical structure of the high molecular weight complex of epidermal growth factor with its binding protein.神经生长因子和表皮生长因子结合蛋白（激肽释放酶）三维结构的预测以及表皮生长因子与其结合蛋白高分子量复合物的假设结构。
Protein Sci. 1993 Aug;2(8):1229-41. doi: 10.1002/pro.5560020805.